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
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Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation.
Kim Van Roey,Bora Uyar,Robert J. Weatheritt,Holger Dinkel,Markus Seiler,Aidan Budd,Toby J. Gibson,Norman E. Davey,Norman E. Davey +8 more
TL;DR: Interaction Modules Directing Cell Regulation Kim Van Roey, Bora Uyar,† Robert J. Weatheritt,‡ Holger Dinkel,† Markus Seiler,† Aidan Budd,† Toby J. Gibson,† and Norman E. Davey*.
Journal ArticleDOI
Tau aggregation is driven by a transition from random coil to beta sheet structure
TL;DR: The abnormal aggregation of the microtubule associated protein tau into paired helical filaments (PHFs) is one the hallmarks of Alzheimer's disease and PHFs aggregated in vitro and in vivo contain beta-sheet structure, as judged by circular dichroismSpectroscopy, Fourier transform infrared (FTIR) spectroscopy and X-ray diffraction.
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Current topics in RNA-protein recognition: control of specificity and biological function through induced fit and conformational capture.
Nicolas Leulliot,Gabriele Varani +1 more
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HMGI/Y proteins: flexible regulators of transcription and chromatin structure.
Raymond Reeves,Lois Beckerbauer +1 more
TL;DR: It may well be that the inherent flexibility of the HMGI/Y proteins, combined with their ability to undergo reversible disordered-to-ordered structural transitions, has been a significant factor in the evolutionary selection of these proteins for their functional role(s) in cells.
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The Klotho proteins in health and disease
Makoto Kuro-o,Makoto Kuro-o +1 more
TL;DR: Growing evidence suggests that the FGF–Klotho endocrine system also has a crucial role in the pathophysiology of ageing-related disorders, including diabetes, cancer, arteriosclerosis and chronic kidney disease; investigation of the crystal structures of FGF-Klitho–FGFR complexes is paving the way for the development of drugs that can regulate these axes.
References
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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
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.
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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.