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
Structural disorder in viral proteins
TL;DR: This paper presents a meta-modelling system that automates the very labor-intensive and therefore time-heavy and therefore expensive and expensive process of manually cataloging and cataloging the components of a molecule.
Journal ArticleDOI
Tandem and cryptic amino acid repeats accumulate in disordered regions of proteins
Michelle Simon,John M. Hancock +1 more
TL;DR: The relationship between AAR frequency and evolution and their localization within proteins based on a set of 5,815 orthologous proteins from four mammalian and a bird genome is investigated.
Journal ArticleDOI
Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation
José Antonio Encinar,Gustavo V. Mallo,Cynthia Mizyrycki,Luciana E. Giono,José M. González-Ros,Manuel Rico,Eduardo T. Cánepa,Silvia N.J. Moreno,José L. Neira,Juan L. Iovanna +9 more
TL;DR: Although there is not a high sequence homology with HMG-I/Y proteins, hp8 can be considered as a HMG/Y-like protein, as shown by the changes in circular dichroism spectra, and gel shift analysis.
Journal ArticleDOI
Genome‐scale prediction of proteins with long intrinsically disordered regions
TL;DR: This first‐of‐its‐kind large‐scale functional analysis shows that proteins with long disordered regions are enriched in a number of cellular functions and processes including certain binding events, regulation of catalytic activities, cellular component organization, biogenesis, biological regulation, and some metabolic and developmental processes.
Journal ArticleDOI
Eukaryotic transcription factors: paradigms of protein intrinsic disorder
Lasse Staby,Charlotte O'Shea,Martin Willemoës,Frederik Theisen,Birthe B. Kragelund,Karen Skriver +5 more
TL;DR: This review focuses on molecular aspects of TFs, which represent paradigms of ID-related features and describes how classic biochemical concepts like allostery, conformational selection, induced fit, and feedback regulation are undergoing a revival with the appreciation of ID.
References
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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.
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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.
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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.
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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.
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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.