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
Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes.
Chad Haynes,Christopher J. Oldfield,Fei Ji,Niels Klitgord,Michael E. Cusick,Predrag Radivojac,Vladimir N. Uversky,Vladimir N. Uversky,Marc Vidal,Lilia M. Iakoucheva +9 more
TL;DR: The results of this study demonstrate that intrinsic structural disorder is a distinctive and common characteristic of eukaryotic hub proteins, and that disorder may serve as a determinant of protein interactivity.
Journal ArticleDOI
Kinetics of Protein-DNA Interaction: Facilitated Target Location in Sequence-Dependent Potential
Michael Slutsky,Leonid A. Mirny +1 more
TL;DR: A search-and-fold mechanism that involves the coupling of protein binding and partial protein folding is proposed that has several important biological implications for search in the presence of other proteins and nucleosomes, simultaneous search by several proteins, etc.
Journal ArticleDOI
Predicting Protein Disorder for N-, C-, and Internal Regions.
TL;DR: Logistic regression, discriminant analysis, and neural networks were used to predict ordered and disordered regions in proteins to support the hypothesis that disorder is encoded by the amino acid sequence.
Journal ArticleDOI
The role of structural disorder in the function of RNA and protein chaperones
Peter Tompa,Peter Csermely +1 more
TL;DR: Evidence is given for the prevalence of functional regions without a well‐defined 3‐D structure in RNA and protein chaperones and a novel “entropy transfer” model is presented to account for the mechanistic role of structural disorder in chaperone function.
Journal ArticleDOI
Prediction of Protein Binding Regions in Disordered Proteins
TL;DR: Scanning several hundred proteomes showed that the occurrence of disordered binding sites increased with the complexity of the organisms even compared to disordered regions in general, and the length distribution of binding sites was different from disordered protein regions ingeneral and was dominated by shorter segments.
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.
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.
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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.