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
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Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits
TL;DR: The notion that oligomer-membrane interaction, disruption of membrane integrity and cell impairment results from both oligomer and membrane biophysical features can be the result of the interplay of these events can help explaining the variable vulnerability of different cell types to the same amyloids and the lack of relation between amyloid load and severity of clinical symptoms.
Journal ArticleDOI
Functional roles of transiently and intrinsically disordered regions within proteins
TL;DR: This review represents some of the key functions of transiently and intrinsically disordered protein regions, which are induced by transient alterations in protein environment or by modification of protein structure, that possess very different functional repertoires.
Journal Article
The roles of intrinsic disorder in protein interaction networks
TL;DR: This review examines the roles of intrinsic disorder in protein network architecture and shows that there are three general ways that intrinsic disorder can contribute: First, intrinsic Disorder can serve as the structural basis for hub protein promiscuity; secondly, intrinsically disordered proteins can bind to structured hub proteins; and thirdly, intrinsic disorderCan provide flexible linkers between functional domains with the linkers enabling mechanisms that facilitate binding diversity.
Journal ArticleDOI
Expanding the proteome: disordered and alternatively folded proteins.
TL;DR: This review provides a survey of recent new directions in the role not only of intrinsically disordered proteins but also of partially structured and highly dynamic members of the disorder–order continuum.
Journal ArticleDOI
Intrinsic Disorder in the Protein Data Bank
Tanguy Le Gall,Pedro Romero,Marc S. Cortese,Vladimir N. Uversky,Vladimir N. Uversky,A. Keith Dunker +5 more
TL;DR: This study compares the amino-acid sequences of proteins whose structures are determined by X-ray crystallography with the corresponding sequences from the Swiss-Prot database and showed that completely ordered proteins are not highly abundant in PDB and many PDB sequences have disordered regions.
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.