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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

Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max)--an in situ spectroscopic study.

TL;DR: It is proposed that during heating the core beta-barrel structure remains intact, but that the interface between the beta-domains melts, revealing hydrophobic faces which may then form new structures in a gel-network.
Journal ArticleDOI

New insight into the solution structures of wheat gluten proteins from Raman optical activity.

TL;DR: Application of a pattern recognition technique, based on principal component analysis (PCA), to the ROA spectra reinforces these conclusions that A-gliadin contains a considerable amount of hydrated alpha-helix, most of which probably lies within a relatively structured C-terminal domain.
Patent

Binding fusion proteins, binding fusion protein-drug conjugates, xten-drug conjugates and methods of making and using same

TL;DR: In this article, the binding fusion protein compositions comprising targeting moieties linked to extended recombinant polypeptide (XTEN) are described, and methods of using such compositions in treatment of diseases, disorders, and conditions.

Visions & Reflections Disordered RNA chaperone proteins: from functions to disease +

TL;DR: RNA chaperones are ubiquitous proteins that play pivotal roles in cellular RNA metabolism and RNA virus replication and it is proposed that they act by organizing complex and highly dynamic networks of RNA-RNA, RNA-protein and protein-protein interactions.
Book ChapterDOI

Protein intrinsic disorder and structure-function continuum.

TL;DR: A correlation between between protein structure and function is described by a more general "protein structure-function continuum" model, where a given protein exists as a dynamic conformational ensemble containing multiple proteoforms characterized by a broad spectrum of structural features and possessing various functional potentials.
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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