The Current Opinion journals were developed out of the recognition that it is increasingly difficult for specialists to keep up to date with the expanding volume of information published in their subject. Elsevier’s Current Opinion journals comprise of 17 leading titles in life sciences and adjacent fields.

Current Opinion in Structural Biology

5-Year Impact Factor: 8.077
Issues per year: 6 issues
Editorial Board

Current Opinion in Structural Biology

Current Opinion in Structural Biology aims to stimulate scientifically grounded, interdisciplinary, multi-scale debate and exchange of ideas. It contains polished, concise and timely reviews and opinions, with particular emphasis on those articles published in the past two years. In addition to describing recent trends, the authors are encouraged to give their subjective opinion of the topics discussed.

In Current Opinion in Structural Biology we help the reader by providing in a systematic manner:

1. The views of experts on current advances in their field in a clear and readable form.
2. Evaluations of the most interesting papers, annotated by experts, from the great wealth of original publications.

Current Opinion in Structural Biology will serve as an invaluable source of information for researchers, lecturers, teachers, professionals, policy makers and students.

Division of the subject into sections

The subject of Structural Biology is divided into twelve themed sections, each of which is reviewed once a year. Each issue contains two sections, and the amount of space devoted to each section is related to its importance.

  • Folding and Binding
  • Nucleic acids and their protein complexes
  • Macromolecular Machines
  • Theory and Simulation
  • Sequences and Topology
  • New constructs and expression of proteins
  • Membranes
  • Engineering and Design
  • Carbohydrate-protein interactions and glycosylation
  • Biophysical and molecular biological methods
  • Multi-protein assemblies in signalling
  • Catalysis and Regulation

Selection of topics to be reviewed

Section Editors, who are major authorities in the field, are appointed by the Editors of the journal. They divide their section into a number of topics, ensuring that the field is comprehensively covered and that all issues of current importance are emphasised. Section Editors commission reviews from authorities on each topic that they have selected. The Editorial Board provides support to the Editors and the Section Editors with their comments and suggestions on names and topics.

Review articles in Current Opinion in Structural Biology are by invitation only.

Review Articles

Authors write short review articles in which they present recent developments in their subject, emphasizing the aspects that, in their opinion, are most important. In addition, they provide short annotations to the papers that they consider to be most interesting from all those published in their topic over the previous two years.

Editorial Overview

Section Editors write a short overview at the beginning of the section to introduce the reviews and to draw the reader's attention to any particularly interesting developments.

This successful format has made Current Opinion in Structural Biology one of the most highly regarded review journals in the field with an Impact factor of 9.344.

Best Cited over the last year.

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SF1 and SF2 helicases: Family matters

Helicases of the superfamily (SF) 1 and 2 are involved in virtually all aspects of RNA and DNA metabolism. SF1 and SF2 helicases share a catalytic core with high structural similarity, but different enzymes even within each SF perform a wide spectrum of distinct functions on diverse substrates. To rationalize similarities and differences between these helicases, we outline a classification based on protein families that are characterized by typical sequence, structural, and mechanistic…

Volume 20, Issue 3, 01 June 2010, Pp 313-324
Margaret E. Fairman-Williams | Ulf Peter Guenther | Eckhard Jankowsky

Mechanisms and principles of N-linked protein glycosylation

N-linked glycosylation, a protein modification system present in all domains of life, is characterized by a high structural diversity of N-linked glycans found among different species and by a large number of proteins that are glycosylated. Based on structural, functional, and phylogenetic approaches, this review discusses the highly conserved processes that are at the basis of this unique general protein modification system. © 2011 Elsevier Ltd.

Volume 21, Issue 5, 01 October 2011, Pp 576-582
Flavio Schwarz | Markus Aebi

Models of macromolecular crowding effects and the need for quantitative comparisons with experiment

In recent years significant effort has been devoted to exploring the potential effects of macromolecular crowding on protein folding and association phenomena. Theoretical calculations and molecular simulations have, in particular, been exploited to describe aspects of protein behavior in crowded and confined conditions and many aspects of the simulated behavior have reflected, at least at a qualitative level, the behavior observed in experiments. One major and immediate challenge for the…

Volume 20, Issue 2, 01 April 2010, Pp 196-206
Adrian H. Elcock

Intrinsically disordered proteins: Regulation and disease

Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions because disordered segments permit interaction with several proteins and hence the re-use of the same protein in multiple pathways. Understanding IDP regulation is important because altered expression of IDPs is associated with many diseases. Recent studies show that IDPs are tightly regulated and that dosage-sensitive genes encode proteins with disordered segments. The tight regulation of IDPs may…

Volume 21, Issue 3, 01 June 2011, Pp 432-440
M. Madan Babu | Robin van der Lee | Natalia Sanchez de Groot | Jörg Gsponer

Unstructural biology coming of age

It is now generally accepted that many proteins or protein domains (intrinsically disordered proteins, IDPs) lack a well-defined tertiary structure under functional conditions. Due to recent concerted activity, a critical transition in this field is gaining momentum, in which qualitative observations are turned into quantitative structural models of IDPs. Here, it is suggested that the transition is set up by the synergy of: (i) more advanced bioinformatic tools for the prediction of disorder…

Volume 21, Issue 3, 01 June 2011, Pp 419-425
Peter Tompa

Nonribosomal peptide synthetases: Structures and dynamics

Nonribosomal peptide synthetases (NRPSs) are large multimodular biocatalysts that utilize complex regiospecific and stereospecific reactions to assemble structurally and functionally diverse peptides that have important medicinal applications. During this ribosome-independent peptide synthesis, catalytic domains of NRPS select, activate or modify the covalently tethered reaction intermediates to control the iterative chain elongation process and product release. Recent advances in structural…

Volume 20, Issue 2, 01 April 2010, Pp 234-240
Matthias Strieker | Alan Tanović | Mohamed A. Marahiel

Alchemical free energy methods for drug discovery: Progress and challenges

Improved rational drug design methods are needed to lower the cost and increase the success rate of drug discovery and development. Alchemical binding free energy calculations, one potential tool for rational design, have progressed rapidly over the past decade, but still fall short of providing robust tools for pharmaceutical engineering. Recent studies, especially on model receptor systems, have clarified many of the challenges that must be overcome for robust predictions of binding affinity…

Volume 21, Issue 2, 01 April 2011, Pp 150-160
John D. Chodera | David L. Mobley | Michael R. Shirts | Richard W. Dixon | Kim Branson | Vijay S. Pande

Structural biology in fragment-based drug design

Fragment-based ligand screening is now established as an emerging paradigm for drug discovery. Here we examine the recent literature looking at how structural biology has been used in a variety of successful fragment-screening applications. We argue that the determination of experimental binding modes has proved to be one of the mainstays of successful fragment-based approaches and that this reflects the difficulty in optimising a fragment to a lead molecule in the absence of structural…

Volume 20, Issue 4, 01 August 2010, Pp 497-507
Christopher W. Murray | Tom L. Blundell

Recognition of nuclear targeting signals by Karyopherin-β proteins

The Karyopherin-β family of nuclear transport factors mediates the majority of nucleocytoplasmic transport. Although each of the 19 Karyopherin-βs transports unique sets of cargos, only three classes of nuclear localization and export signals, or NLSs and NESs, have been characterized. The short basic classical-NLS was first discovered in the 1980s and their karyopherin-bound structures were first reported more than 10 years ago. More recently, structural and biophysical studies of…

Volume 20, Issue 6, 01 December 2010, Pp 782-790
Darui Xu | Alicia Farmer | Yuh Min Chook

Mass spectrometry: Come of age for structural and dynamical biology

Over the past two decades, mass spectrometry (MS) has emerged as a bone fide approach for structural biology. MS can inform on all levels of protein organization, and enables quantitative assessments of their intrinsic dynamics. The key advantages of MS are that it is a sensitive, high-resolution separation technique with wide applicability, and thereby allows the interrogation of transient protein assemblies in the context of complex mixtures. Here we describe how molecular-level information…

Volume 21, Issue 5, 01 October 2011, Pp 641-649
Justin L P Benesch | Brandon T. Ruotolo

Structural insights into agonist-induced activation of G-protein-coupled receptors

Recent years have seen tremendous breakthroughs in structure determination of G-protein-coupled receptors (GPCRs). In 2011, two agonist-bound active-state structures of rhodopsin have been published. Together with structures of several rhodopsin activation intermediates and a wealth of biochemical and spectroscopic information, they provide a unique structural framework on which to understand GPCR activation. Here we use this framework to compare the recent crystal structures of the…

Volume 21, Issue 4, 01 August 2011, Pp 541-551
Xavier Deupi | Jörg Standfuss

Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses

Small molecules that bind to normally unoccupied thyroxine (T4) binding sites within transthyretin (TTR) in the blood stabilize the tetrameric ground state of TTR relative to the dissociative transition state and dramatically slow tetramer dissociation, the rate-limiting step for the process of amyloid fibril formation linked to neurodegeneration and cell death. These so-called TTR kinetic stabilizers have been designed using structure-based principles and one of these has recently been shown…

Volume 20, Issue 1, 01 February 2010, Pp 54-62
Stephen Connelly | Sungwook Choi | Steven M. Johnson | Jeffery W. Kelly | Ian A. Wilson

Protein dynamics and allostery: An NMR view

Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link between internal motions over a wide range of time scales and function in protein-ligand interactions. Proteins respond to…

Volume 21, Issue 1, 01 February 2011, Pp 62-67
Shiou Ru Tzeng | Charalampos G. Kalodimos

Constructing ensembles for intrinsically disordered proteins

The relatively flat energy landscapes associated with intrinsically disordered proteins makes modeling these systems especially problematic. A comprehensive model for these proteins requires one to build an ensemble consisting of a finite collection of structures, and their corresponding relative stabilities, which adequately capture the range of accessible states of the protein. In this regard, methods that use computational techniques to interpret experimental data in terms of such ensembles…

Volume 21, Issue 3, 01 June 2011, Pp 426-431
Charles K. Fisher | Collin M. Stultz

Advances in RNA structure analysis by chemical probing

RNA is arguably the most versatile biological macromolecule because of its ability both to encode and to manipulate genetic information. The diverse roles of RNA depend on its ability to fold back on itself to form biologically functional structures that bind small molecule and large protein ligands, to change conformation, and to affect the cellular regulatory state. These features of RNA biology can be structurally interrogated using chemical mapping experiments. The usefulness and…

Volume 20, Issue 3, 01 June 2010, Pp 295-304
Kevin M. Weeks

Nanobody stabilization of G protein-coupled receptor conformational states

Remarkable progress has been made in the field of G protein-coupled receptor (GPCR) structural biology during the past four years. Several obstacles to generating diffraction quality crystals of GPCRs have been overcome by combining innovative methods ranging from protein engineering to lipid-based screens and microdiffraction technology. The initial GPCR structures represent energetically stable inactive-state conformations. However, GPCRs signal through different G protein isoforms or G…

Volume 21, Issue 4, 01 August 2011, Pp 567-572
Jan Steyaert | Brian K. Kobilka

Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering

Small-angle X-ray scattering (SAXS) is changing how we perceive biological structures, because it reveals dynamic macromolecular conformations and assemblies in solution. SAXS information captures thermodynamic ensembles, enhances static structures detailed by high-resolution methods, uncovers commonalities among diverse macromolecules, and helps define biological mechanisms. SAXS-based experiments on RNA riboswitches and ribozymes and on DNA-protein complexes including DNA-PK and p53 discover…

Volume 20, Issue 1, 01 February 2010, Pp 128-137
Robert P. Rambo | John A. Tainer

Protein binding specificity versus promiscuity

Interactions between macromolecules in general, and between proteins in particular, are essential for any life process. Examples include transfer of information, inhibition or activation of function, molecular recognition as in the immune system, assembly of macromolecular structures and molecular machines, and more. Proteins interact with affinities ranging from millimolar to femtomolar and, because affinity determines the concentration required to obtain 50% binding, the amount of different…

Volume 21, Issue 1, 01 February 2011, Pp 50-61
Gideon Schreiber | Amy E. Keating

Structural studies on human 2-oxoglutarate dependent oxygenases

2-Oxoglutarate and ferrous iron-dependent oxygenases have emerged as an important family of human enzymes that catalyse hydroxylations and related demethylation reactions. Their substrates in humans include proteins, nucleic acids, lipids and small molecules. They play roles in collagen biosynthesis, hypoxic sensing, regulation of gene expression and lipid biosynthesis/metabolism. Structural analyses, principally employing crystallography, have revealed that all of these oxygenases possess a…

Volume 20, Issue 6, 01 December 2010, Pp 659-672
Michael A. McDonough | Christoph Loenarz | Rasheduzzaman Chowdhury | Ian J. Clifton | Christopher J. Schofield

Large conformational changes in proteins: Signaling and other functions

Guanine and adenine nucleotide triphosphatases, such as Ras proteins and protein kinases, undergo large conformational changes upon ligand binding in the course of their functions. New computer simulation methods have combined with experimental studies to deepen our understanding of these phenomena. In particular, a 'conformational selection' picture is emerging, where alterations in the relative populations of pre-existing conformations can best describe the conformational switching activity…

Volume 20, Issue 2, 01 April 2010, Pp 142-147
Barry J. Grant | Alemayehu A. Gorfe | J. Andrew McCammon

To milliseconds and beyond: Challenges in the simulation of protein folding

Quantitatively accurate all-atom molecular dynamics (MD) simulations of protein folding have long been considered a holy grail of computational biology. Due to the large system sizes and long timescales involved, such a pursuit was for many years computationally intractable. Further, sufficiently accurate forcefields needed to be developed in order to realistically model folding. This decade, however, saw the first reports of folding simulations describing kinetics on the order of milliseconds,…

Volume 23, Issue 1, 01 February 2013, Pp 58-65
Thomas J. Lane | Diwakar Shukla | Kyle A. Beauchamp | Vijay S. Pande

Structural assembly of cullin-RING ubiquitin ligase complexes

The cullin-RING ubiquitin ligases (CRLs) are the largest family of multi-subunit E3 ligases in eukaryotes, which ubiquitinate protein substrates in numerous cellular pathways. CRLs share a common arched scaffold and a RING domain catalytic subunit, but use different adaptors and substrate receptors to assemble unique E3 machineries. In comparison to the first CRL structure, recent findings have revealed increased complexity in the overall architecture and assembly mode of CRLs, including…

Volume 20, Issue 6, 01 December 2010, Pp 714-721
Erik S. Zimmerman | Brenda A. Schulman | Ning Zheng

Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy

Nine different near-atomic resolution structures of icosahedral viruses, determined by electron cryo-microscopy and published between early 2008 and late 2010, fulfil predictions made 15 years ago that single-particle cryo-EM techniques could visualize molecular detail at 3-4. Å resolution. This review summarizes technical developments, both in instrumentation and in computation, that have led to the new structures, which advance our understanding of virus assembly and cell entry. © 2011…

Volume 21, Issue 2, 01 April 2011, Pp 265-273
Nikolaus Grigorieff | Stephen C. Harrison

Coarse-grained models for protein aggregation

The aggregation of soluble proteins into fibrillar species is a complex process that spans many lengths and time scales, and that involves the formation of numerous on-pathway and off-pathway intermediate species. Despite this complexity, several elements underlying the aggregation process appear to be universal. The kinetics typically follows a nucleation-growth process, and proteins with very different sequences aggregate to form similar fibril structures, populating intermediates with…

Volume 21, Issue 2, 01 April 2011, Pp 209-220
Chun Wu | Joan Emma Shea

Structural regulation of cullin-RING ubiquitin ligase complexes

Cullin-RING ligases (CRLs) compose the largest class of E3 ubiquitin ligases. CRLs are modular, multisubunit enzymes, comprising interchangeable substrate receptors dedicated to particular Cullin-RING catalytic cores. Recent structural studies have revealed numerous ways in which CRL E3 ligase activities are controlled, including multimodal E3 ligase activation by covalent attachment of the ubiquitin-like protein NEDD8, inhibition of CRL assembly/activity by CAND1, and several mechanisms of…

Volume 21, Issue 2, 01 April 2011, Pp 257-264
David M. Duda | Daniel C. Scott | Matthew F. Calabrese | Erik S. Zimmerman | Ning Zheng | Brenda A. Schulman