Journal ArticleDOI
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Peter E. Wright,H. Jane Dyson +1 more
TLDR
Many proteins that lack intrinsic globular structure under physiological conditions have now been recognized, and it appears likely that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions.About:
This article is published in Journal of Molecular Biology.The article was published on 1999-10-22. It has received 2804 citations till now. The article focuses on the topics: Protein structure function & Intrinsically disordered proteins.read more
Citations
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Journal ArticleDOI
Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases
Vladimir N. Uversky,Vrushank Davé,Lilia M. Iakoucheva,Prerna Malaney,Steven J. Metallo,Ravi Ramesh Pathak,Andreas C. Joerger +6 more
TL;DR: The ability of these proteins to return to highly flexible conformations after the completion of a particular function, and their predisposition to adopt different conformations depending on their environment, are unique physiological properties of IDPs that allow them to exert different functions in different cellular contexts according to a specific conformational state.
Book ChapterDOI
Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance.
H.J. Dyson,Peter E. Wright +1 more
TL;DR: New insights have been obtained into the nature of the conformational ensemble and the dynamics of denatured proteins through the application of state-of-the-art heteronuclear NMR methods, which show that the behavior of den atured proteins is typically far from that of a statistical random coil.
Journal ArticleDOI
Structure and Function of a Mitochondrial Late Embryogenesis Abundant Protein Are Revealed by Desiccation
Dimitri Tolleter,Michel Jaquinod,Cécile Mangavel,Catherine Passirani,Patrick Saulnier,Stephen Manon,Emeline Teyssier,Nicole Payet,Marie-Hélène Avelange-Macherel,David Macherel +9 more
TL;DR: It is shown that LEAM, a mitochondrial LEA protein expressed in seeds, is a natively unfolded protein, which reversibly folds into α-helices upon desiccation, and sequence analyses of several homologous proteins suggest a similar protection mechanism likely acts with other types of cellular membranes.
Journal ArticleDOI
Transient protein-protein interactions
TL;DR: An overview of the transient interactions; the importance of transient interactions as drug targets; and the structural characterization of transient protein-protein complexes based on the geometrical and physicochemical features ofThe transient complexes' interfaces are given.
Journal ArticleDOI
The role of disorder in interaction networks: a structural analysis
TL;DR: Surprisingly, it is found that the binding interfaces in single‐ interface hubs are highly structured, as is the case for multi‐interface hubs, suggesting that their binding promiscuity is related to the disorder of their binding partners.
References
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Journal ArticleDOI
The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
TL;DR: It is demonstrated that p300/CBP acetylates nucleosomes in concert with PCAF, a novel class of acetyltransferases in that it does not have the conserved motif found among various other acetyl transferases.
Journal ArticleDOI
The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen
Andrew K. Shiau,Danielle Barstad,Paula M. Loria,Lin Cheng,Peter J. Kushner,David A. Agard,Geoffrey L. Greene +6 more
TL;DR: Crystal structures of the human estrogen receptor alpha (hER alpha) ligand-binding domain (LBD) and the OHT-LBD complex reveal the two distinct mechanisms by which structural features of OHT promote this "autoinhibitory" helix 12 conformation.
Journal ArticleDOI
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
TL;DR: The X-ray crystal structure of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins.
Journal ArticleDOI
Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
Keh-Ming Pan,Michael J. Baldwin,J Nguyen,María Gasset,Ana Serban,Darlene Groth,Ingrid Mehlhorn,Ziwei Huang,Robert J. Fletterick,Fred E. Cohen +9 more
TL;DR: It is argued that the conversion of alpha-helices into beta-sheets underlies the formation of PrPSc, and it is likely that this conformational transition is a fundamental event in the propagation of prions.
Journal ArticleDOI
A signature motif in transcriptional co-activators mediates binding to nuclear receptors.
TL;DR: It is proposed that the LXXLL motif is a signature sequence that facilitates the interaction of different proteins with nuclear receptors, and is thus a defining feature of a new family of nuclear proteins.