Current Opinion in Structural Biology (CURR OPIN STRUC BIOL )

Publisher: Elsevier

Description

Current Opinion in Structural Biology contains: Over 90 reviews from leading international contributors Web alerts of hot sites Paper alert service - the latest exciting papers Evaluated reference lists for all articles Annual author and subject index Online Fully searchable Access back issues Numerous links Search and read all issues published since 1984, giving you access to your own reference library without leaving your desk. Save valuable time by exploring our links to MEDLINE and numerous websites. Check out contents and abstracts FREE

  • Impact factor
    8.74
  • 5-year impact
    9.02
  • Cited half-life
    7.20
  • Immediacy index
    1.45
  • Eigenfactor
    0.04
  • Article influence
    4.60
  • Website
    Current Opinion in Structural Biology website
  • Other titles
    Bibliography of the current world literature., Current opinion in structural biology, Structural biology
  • ISSN
    1879-033X
  • OCLC
    23812553
  • Material type
    Periodical, Internet resource
  • Document type
    Journal / Magazine / Newspaper, Internet Resource

Publisher details

Elsevier

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Pre-print allowed on any website or open access repository
    • Voluntary deposit by author of authors post-print allowed on authors' personal website, arXiv.org or institutions open scholarly website including Institutional Repository, without embargo, where there is not a policy or mandate
    • Deposit due to Funding Body, Institutional and Governmental policy or mandate only allowed where separate agreement between repository and the publisher exists.
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months .
    • Set statement to accompany deposit
    • Published source must be acknowledged
    • Must link to journal home page or articles' DOI
    • Publisher's version/PDF cannot be used
    • Articles in some journals can be made Open Access on payment of additional charge
    • NIH Authors articles will be submitted to PubMed Central after 12 months
    • Publisher last contacted on 18/10/2013
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Many proteins require help from metal cofactors to function properly. Due to the involvement of metal binding, folding of these metalloproteins can be much more complicated. In recent years, several computational methods have been developed to reveal the essential features of metal-coupled protein folding, ranging from quantum mechanics (QM) to atomistic and coarse-grained (CG) simulations. These theoretical tools have achieved great successes in solving the multiscale difficulties arising from metal binding, and provided new insights into the mechanisms of metalloprotein folding. In this review, we first discuss the interaction features of metal-coordination and then introduce several computational models and their applications in metal-coupled folding. Finally we discuss the effects of metal-binding on the protein energy landscape, which is followed by some perspectives. Copyright © 2014 The Authors. Published by Elsevier Ltd.. All rights reserved.
    Current Opinion in Structural Biology 02/2015; 30.
  • [Show abstract] [Hide abstract]
    ABSTRACT: Classically, allostery induces a functional switch through a conformational change. However, lately an increasing number of studies concluded that the allostery they observe takes place through sheer dynamics. Here we explain that even if a structural comparison between the active and inactive states does not detect a conformational change, it does not mean that there is no conformational change. We list likely reasons for this lack of observation, including crystallization conditions and crystal effects; one of the states is disordered; the structural comparisons disregard the quaternary protein structure; overlooking synergy effects among allosteric effectors and graded incremental switches and too short molecular dynamics simulations. Specific functions are performed by distinct conformations; they emerge through specific interactions between conformationally selected states. Copyright © 2014 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 12/2014; 30C:17-24.
  • Current Opinion in Structural Biology 12/2014;
  • [Show abstract] [Hide abstract]
    ABSTRACT: The recent structure of a truncated mTOR in a complex with mLST8 has provided a basic framework for understanding all of the phosphoinositide 3-kinase (PI3K)-related kinases (PIKKs): mTOR, ATM, ATR, SMG-1, TRRAP and DNA-PK. The PIKK kinase domain is encircled by the FAT domain, a helical solenoid that is present in all PIKKs. PIKKs also have an extensive helical solenoid N-terminal to the FAT domain for which there is limited structural information. This N-terminal helical solenoid is essential for binding proteins that associate with the PIKKs to regulate their activity and cellular localization. Copyright © 2014 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 12/2014; 29C:134-142.
  • [Show abstract] [Hide abstract]
    ABSTRACT: Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding conducted in cells and in vitro under crowded conditions. Many of the observations can be understood in terms of interactions between proteins and the rest of the intracellular environment (i.e. quinary interactions). Nevertheless, NMR studies of folding and binding in cells and cell-like environments remain in their infancy. The frontier involves investigations of larger proteins and further efforts in higher eukaryotic cells. Copyright © 2014 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 12/2014; 30C:7-16.
  • Current Opinion in Structural Biology 12/2014; 29C:vi-viii.
  • [Show abstract] [Hide abstract]
    ABSTRACT: Structure and binding of lipid-modified Wnt8 with Frizzled8 cysteine-rich domain.•Modularity of Wnt inhibitory factor 1 combining Wnt-binding and heparan sulphate-binding.•Integration of multiple interaction sites in LRP5/6 ectodomain architecture.•Ternary complex assembly of RNF43/ZNRF3 and LGR4/5/6 bridged by R-spondin.•Ectodomain dimerisation of the Frizzled-specific E3 ligase ZNRF3.
    Current Opinion in Structural Biology 12/2014; 29.
  • [Show abstract] [Hide abstract]
    ABSTRACT: Several studies suggest flexible linkage between extracellular and intracellular regions.•Others imply more rigid connections, required for allosteric regulation of dimers.•Interactions with membrane lipids play important roles in EGFR regulation.•Cellular studies suggest half-of-the-sites negative cooperativity for human EGFR.
    Current Opinion in Structural Biology 12/2014; 29.
  • [Show abstract] [Hide abstract]
    ABSTRACT: A conserved, ultrasensitive, ultrastable chemosensory array guides bacterial motility.•Three core proteins form the array framework: receptor, His-kinase, and adaptor.•Complementary approaches are developing a molecular model of array architecture.•Recent progress has furthered the mechanistic understanding of receptor signaling.•Early studies are investigating the mechanism of kinase on-off switching.
    Current Opinion in Structural Biology 12/2014; 29.
  • [Show abstract] [Hide abstract]
    ABSTRACT: The biosynthetic pathways for patellamide and related natural products have recently been studied by structural biology. These pathways produce molecules that have a complex framework and exhibit a diverse array of activity due to the variability of the amino acids that are found in them. As these molecules are difficult to synthesize chemically, exploitation of their properties has been modest. The patellamide pathway involves amino acid heterocyclization, peptide cleavage, peptide macrocyclization, heterocycle oxidation and epimerization; closely related products are also prenylated. Enzyme activities have been identified for all these transformations except epimerization, which may be spontaneous. This review highlights the recent structural and mechanistic work on amino acid heterocyclization, peptide cleavage and peptide macrocyclization. This work should help in using the enzymes to produce novel analogs of the natural products enabling an exploitation of their properties. Copyright © 2014. Published by Elsevier Ltd.
    Current Opinion in Structural Biology 11/2014; 29C:112-121.
  • [Show abstract] [Hide abstract]
    ABSTRACT: Although general principles of enzyme catalysis are fairly well understood nowadays, many important details of how exactly the substrate is bound and processed in an enzyme remain often invisible and as such elusive. In fortunate cases, structural analysis of enzymes can be accomplished at true atomic resolution thus making possible to shed light on otherwise concealed fine-structural traits of bound substrates, intermediates, cofactors and protein groups. We highlight recent structural studies of enzymes using ultrahigh-resolution X-ray protein crystallography showcasing its enormous potential as a tool in the elucidation of enzymatic mechanisms and in unveiling fundamental principles of enzyme catalysis. We discuss the observation of seemingly hyper-reactive, physically distorted cofactors and intermediates with elongated scissile substrate bonds, the detection of 'hidden' conformational and chemical equilibria and the analysis of protonation states with surprising findings. In delicate cases, atomic resolution is required to unambiguously disclose the identity of atoms as demonstrated for the metal cluster in nitrogenase. In addition to the pivotal structural findings and the implications for our understanding of enzyme catalysis, we further provide a practical framework for resolution enhancement through optimized data acquisition and processing. Copyright © 2014 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 11/2014;
  • Current Opinion in Structural Biology 11/2014;
  • [Show abstract] [Hide abstract]
    ABSTRACT: Arf GTPases are major regulators of membrane traffic and organelle structure in eukaryotes where they recruit many different effectors, including components of vesicular coats, proteins that tether membranes, sort lipids or have diverse other functions in vesicular traffic, and bacterial proteins that divert Arf functions in host cells. A dozen of structures of unrelated effectors bound to Arf1, Arf6 or their close relative Arl1 are available, revealing that Arf GTPases do not recognize preferred structures in their effectors. In contrast, a trait common to many Arf/effector complexes is that they are juxtaposed to membranes by multiple protein/membrane contacts, yet of diverse sizes, shapes and physicochemistry. The common function of Arf GTPases thus appears to be their ability to assemble versatile, multivalent membrane-binding platforms, resulting in optimal orientation and allosteric regulation of their effectors leading to a plethora of membrane-localized functions. Copyright © 2014 Elsevier Ltd. All rights reserved.
    Current Opinion in Structural Biology 11/2014;
  • [Show abstract] [Hide abstract]
    ABSTRACT: Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.
    Current Opinion in Structural Biology 10/2014; 29:58–66.
  • [Show abstract] [Hide abstract]
    ABSTRACT: UVR8 is a UV-B photoreceptor that employs specific tryptophans in its primary sequence as chromophores in photoreception. UV-B absorption causes dissociation of the dimeric photoreceptor by neutralizing interactions between monomers. The monomeric form initiates signalling through interaction with the COP1 protein, leading to transcriptional responses. This article discusses the structural basis of UVR8 function, highlighting recent research on the mechanism of photoreception and on interactions with other proteins involved in signalling and regulation.
    Current Opinion in Structural Biology 10/2014; 29:52–57.
  • Current Opinion in Structural Biology 10/2014;
  • [Show abstract] [Hide abstract]
    ABSTRACT: Membrane fusion is essential for cellular transport in eukaryotes. Abnormalities contribute to a wide range of diseases including diabetes and neurological disorders. A key regulator of SNARE-mediated membrane fusion is the Sec1/Munc18 (SM) protein family. Universal structural features of SM proteins have been identified that affect the way these interact with their partner Syntaxin SNARE proteins. Whilst the molecular basis for SM-regulated SNARE complex formation has been extensively studied, it remains poorly understood. Recent crystal structures of SM proteins alone or in complex have provided new insight. Here we examine the available structural information on SM proteins for clues to how these enigmatic proteins might regulate SNARE complex assembly and membrane fusion.
    Current Opinion in Structural Biology 10/2014; 29:44–51.