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Journal ArticleDOI

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

Peter E. Wright, +1 more
- 22 Oct 1999 - 
- Vol. 293, Iss: 2, pp 321-331
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.
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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.

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Citations
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Journal ArticleDOI

A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome.

TL;DR: In this paper, the authors present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species.
Book ChapterDOI

Single-Molecule Fluorescence Studies of Intrinsically Disordered Proteins

TL;DR: It is anticipated that SMF and single-molecule methods will find broad application for structural and mechanistic studies of a wide variety of IDPs, both of their disordered conformations, and their ordered ensembles relevant for function and disease.
Journal ArticleDOI

Intrinsically disordered proteins and multicellular organisms.

TL;DR: It is proposed that an "IDP-based developmental toolkit," which is comprised of IDP regions, PTMs, especially multiplePTMs, within these IDp regions, and AS events within segments of pre-mRNA that code for these same IDP areas, allows functional diversification and environmental responsiveness for molecules that direct the development of complex metazoans.
Journal ArticleDOI

Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins

TL;DR: This review argues that the heterogeneity of disordered segments needs to be taken into account for a better understanding of protein disorder and presents a small survey of current methods to identify disordered proteins or protein segments.
Journal ArticleDOI

The solution structure of acyl carrier protein from Mycobacterium tuberculosis.

TL;DR: The similarity between AcpM and other ACPs reveals the conserved structural motif that is recognized by all type II enzymes, however, the function of the coil domain extending from helix IV to the carboxyl terminus remains enigmatic, but its structural characteristics suggest that it may interact with the very long chain intermediates in mycolic acid biosynthesis or control specific protein-protein interactions.
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

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.

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.
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