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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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The expanding view of protein-protein interactions: Complexes involving intrinsically disordered proteins

TL;DR: This survey examines the basic properties of the complexes of disordered and ordered proteins from three different directions and proposes the generalization of the 'energy landscape model' for the description of complex formation that can help to put the various types of protein associations on a common ground.
Journal ArticleDOI

DFLpred: High-throughput prediction of disordered flexible linker regions in protein sequences

TL;DR: This work conceptualized, developed and empirically assessed a first-of-its-kind sequence-based predictor of DFLs, DFLpred, which outperforms existing alternatives that include methods for the prediction of flexible linkers, flexible residues, intrinsically disordered residues and various combinations of these methods.
Journal ArticleDOI

AMPA‐receptor‐mediated excitatory synaptic transmission is enhanced by iron‐induced α‐synuclein oligomers

TL;DR: In this paper, the neurophysiological effects of various biophysically-characterized preparations of α-synuclein (α-syn) aggregates on excitatory synaptic transmission in autaptic neuronal cultures were studied.
Journal ArticleDOI

Algorithmic approaches to protein-protein interaction site prediction

TL;DR: The intricacies of the biological theory, datasets, and features required for modern protein-protein interaction site (PPIS) prediction are described, and an integrative analysis of the state-of-the-art algorithms and their performance is presented.
Journal ArticleDOI

The Ising model for prediction of disordered residues from protein sequence alone

TL;DR: A new method (IsUnstruct) based on the Ising model for prediction of disordered residues from protein sequence alone has been developed and has been compared with other available methods and found to perform well.
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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