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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

Kinetics of Contact Formation and End-to-End Distance Distributions of Swollen Disordered Peptides

TL;DR: In buffered water, it is found that introducing charges in a glycine-rich sequence induces a mild chain swelling and a significant speed-up of the intrachain dynamics, whereas the removal of the glycines results in almost a two-fold increase of the chain volume and a drastic slowing down.
Journal ArticleDOI

Intrinsically Disordered Proteins: Where Computation Meets Experiment

TL;DR: In this paper, the authors discuss methods for studying intrinsically disordered proteins and provide examples of how computational methods can improve our understanding of IDPs, focusing on two intensely studied proteins that have been implicated in very different pathologic pathways.
Journal ArticleDOI

Regulation of protein phosphatase 1 by intrinsically disordered proteins.

TL;DR: Structural studies highlighting the interaction of these IDP regulatory proteins with PP1 are an attractive model system because it allows general parameters for a group of diverse IDPs that interact with the same binding partner to be identified, while also providing fundamental insights into PP1 biology.
Journal ArticleDOI

The existence of multiple conformers of interleukin-21 directs engineering of a superpotent analogue.

TL;DR: The high resolution three-dimensional structure of human interleukin (hIL)-21 has been resolved by heteronuclear NMR spectroscopy and an hIL-21 analog was designed to stabilize the region around helix C through the introduction of a segment grafted from hil-4.
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Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1

TL;DR: A combined bioinformatics and experimental approach is used to present a model of the stress-associated RCD1-transcription factor interactome and to contribute to the emerging understanding of the interactions between folded hubs and their intrinsically disordered partners.
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.
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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.
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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.

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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