Journal ArticleDOI
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Peter E. Wright,H. Jane Dyson +1 more
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.About:
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.read more
Citations
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Journal ArticleDOI
Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs)
TL;DR: It is found out that intrinsically disordered proteins have unique structural features such as high flexibility and random coil-like conformations which enable them to participate in both the “one to many” and “many to one” interaction.
Journal ArticleDOI
Hydropathy Patterning Complements Charge Patterning to Describe Conformational Preferences of Disordered Proteins.
TL;DR: A new order parameter, sequence hydropathy decoration (SHD), is proposed, which can provide a near quantitative understanding of scaling and structural properties of IDPs devoid of charged residues and is tested against available experimental data and finds a semi-quantitative match in predicting the scaling behavior.
Journal ArticleDOI
Protein folding: binding of conformationally fluctuating building blocks via population selection.
TL;DR: A broad range of observations are presented, showing them to be consistent with the view that binding and folding are similar events, with the differences stemming from different stabilities and hence population times.
Journal ArticleDOI
Computational Prediction of O-linked Glycosylation Sites That Preferentially Map on Intrinsically Disordered Regions of Extracellular Proteins
TL;DR: In this article, a support vector machine (SVM) was applied to predict whether Ser or Thr is glycosylated, in order to elucidate the O-glycosylation mechanism.
Journal ArticleDOI
The unstructured C-terminus of the τ subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the α subunit
Slobodan Jergic,Kiyoshi Ozawa,Neal Kenneth Williams,Xun-Cheng Su,Daniel D Scott,Samir M. Hamdan,Jeffrey A. Crowther,Gottfried Otting,Nicholas E. Dixon +8 more
TL;DR: The data suggest that the unstructured C-terminus of τ becomes folded into a helix–loop–helix in its complex with α, suggesting that the processivity switch of the replisome functionally involves Domain IV of τ.
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
Andrew K. Shiau,Danielle Barstad,Paula M. Loria,Lin Cheng,Peter J. Kushner,David A. Agard,Geoffrey L. Greene +6 more
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.
Journal ArticleDOI
Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
Keh-Ming Pan,Michael J. Baldwin,J Nguyen,María Gasset,Ana Serban,Darlene Groth,Ingrid Mehlhorn,Ziwei Huang,Robert J. Fletterick,Fred E. Cohen +9 more
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.