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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 binding of Maize DHN1 to Lipid Vesicles. Gain of Structure and Lipid Specificity

TL;DR: It is shown that maize (Zea mays) DHN DHN1 can bind to lipid vesicles that contain acidic phospholipids, and that the association ofDHN1 with vesicle results in an apparent increase of α-helicity of the protein.
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FAT: a novel domain in PIK-related kinases

TL;DR: A new subfamily of the PI-kinase superfamily has emerged, called PIK-related, and this domain is referred to as the PIkinase domain because it has proved difficult to define shared domains in the large N-terminal portions.
Journal ArticleDOI

Understanding eukaryotic linear motifs and their role in cell signaling and regulation.

TL;DR: The current state of linear motif biology is summarized, which uses low affinity interactions to create cooperative, combinatorial and highly dynamic regulatory protein complexes, which suggest that models for cell regulatory networks in systems biology should neither be overly dependent on stochastic nor on smooth deterministic approximations.
Journal ArticleDOI

Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.

TL;DR: This review describes some of the most characteristic features of the IDP conformational behavior and the unique response of IDPs to changes in their environment.
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Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life

TL;DR: This work comprehensively characterized intrinsic disorder at proteomic and protein levels from all significant perspectives, including abundance, cellular localization, functional roles, evolution, and impact on structural coverage, and shows that intrinsic disorder is more abundant and has a unique profile in eukaryotes.
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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