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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Preventing α-synuclein aggregation: the role of the small heat-shock molecular chaperone proteins.
TL;DR: How the small heat-shock proteins interact with α-synuclein to prevent its aggregation is discussed and the multi-faceted nature of the mechanisms used by sHsps to prevent the fibrillar aggregation of proteins is highlighted.
Journal ArticleDOI
Multicolor single-molecule FRET to explore protein folding and binding
Yann Gambin,Ashok A. Deniz +1 more
TL;DR: This review provides a brief introduction to the smFRET technique, followed with advanced multicolor measurements and end with ongoing methodology developments in microfluidics and protein labeling that are beginning to make these techniques more broadly applicable to answering a number of key questions about folding and binding.
Journal ArticleDOI
Prediction of peptide structure: how far are we?
Annick Thomas,Sébastien Deshayes,Marc Decaffmeyer,Marie Hélène Van Eyck,Benoit Charloteaux,Robert Brasseur +5 more
TL;DR: The most recent algorithm, PepLook introduces indexes for evaluating structural polymorphism and stability, which should provide new means for the rational design of peptides.
Journal ArticleDOI
Biochemistry. Controlled chaos.
Vladimir N. Uversky,A.K. Dunker +1 more
TL;DR: First, I look across the river at a neighbor’s garden – rich in profusion, it seems a riot of colors and varieties of plant life – vegetables mixed in with flowers, seemingly randomly deposited, helter-skelter, but also artistically clumped.
Journal ArticleDOI
Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome.
Charles A. Galea,Anthony A. High,John C. Obenauer,Ashutosh Mishra,Cheon-Gil Park,Marco Punta,Avner Schlessinger,Jing Ma,Burkhard Rost,Clive A. Slaughter,Richard W. Kriwacki +10 more
TL;DR: While disordered proteins play diverse biological roles in mouse fibroblasts, they do exhibit heightened involvement in several functional categories, including, cytoskeletal structure and cell movement, metabolic and biosynthesis processes, organelle structure, cell division, gene transcription, and ribonucleoprotein complexes.
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.