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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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MobiDB: a comprehensive database of intrinsic protein disorder annotations

TL;DR: MobiDB features experimental annotations for 17 285 proteins, covering the entire PDB and predictions for the SwissProt database, with 565 200 annotated sequences, and a weighted consensus disorder used to classify disordered regions into flexible and constrained disorder.
Journal ArticleDOI

Comprehensive large scale assessment of intrinsic protein disorder.

TL;DR: MobiDB annotates disorder for UniProt sequences, allowing the first large-scale assessment of fast disorder predictors on 25 833 different sequences with X-ray crystallographic structures and produces a comprehensive ranking of predictors.
Journal ArticleDOI

FoldUnfold: web server for the prediction of disordered regions in protein chain

TL;DR: FoldUnfold has been tested on datasets of globular proteins and long disordered protein segments and showed improved performance over some other widely used methods, such as DISOPRED, PONDR VL3H, IUPred and GlobPlot.
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RACK1 has the nerve to act : Structure meets function in the nervous system

TL;DR: New light is shed on both the virtues and the variety of neuronal RACK1 interactions and their physiological consequences, compatible with reports of Rackers modulations in brain ageing and in various neurodegenerative diseases.
Journal ArticleDOI

iPhos-PseEn: identifying phosphorylation sites in proteins by fusing different pseudo components into an ensemble classifier.

TL;DR: A predictor called iPhos-PseEn is developed by fusing four different pseudo component approaches (amino acids’ disorder scores, nearest neighbor scores, occurrence frequencies, and position weights) into an ensemble classifier via a voting system and indicated that the proposed predictor remarkably outperformed its existing counterparts.
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.
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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.
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