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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

Methionine oxidation inhibits fibrillation of human α-synuclein in vitro

TL;DR: The effect of methionine oxidation of human recombinant α‐synuclein on its structural properties and propensity to fibrillate was examined and the addition of oxidized α‐ synuclein to the unoxidized form led to a substantial inhibition of α‐ Synuclein fibrillation.
Journal ArticleDOI

Malleable machines take shape in eukaryotic transcriptional regulation

TL;DR: Determining the functional significance of intrinsically disordered protein regions and developing conceptual models of their action will help to illuminate their key role in transcription regulation.
Journal ArticleDOI

SQ/TQ cluster domains: concentrated ATM/ATR kinase phosphorylation site regions in DNA-damage-response proteins.

TL;DR: Mutational analyses of a number of SCD‐containing proteins indicate that multisite phosphorylation of SQ/TQ motifs is required for normal DNA‐damage responses, most commonly by mediating protein–protein interactions in the formation of DNA‐ damage‐induced complexes.
Proceedings ArticleDOI

The protein non-folding problem: amino acid determinants of intrinsic order and disorder.

TL;DR: To investigate the determinants of protein order and disorder, three primary and one derivative database of intrinsically disordered proteins were compiled, suggesting that disorder in all 3 databases is very similar, but with those characterized by NMR and CD being the most similar, those by CD and X-ray being the least similar.
Journal ArticleDOI

Binding-induced folding of a natively unstructured transcription factor.

TL;DR: This study studies the folding and binding of the pKID domain of CREB to the KIX domain of the co-activator CBP, and helps explain how being unstructured can confer an advantage in protein target recognition.
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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