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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Structural and energetic basis of allostery.
TL;DR: Using an ensemble-based model, it is shown that allosteric phenomena can be formulated in terms of conformational free energies of the cooperative elements in a protein and the coupling interactions between them, and provides insights into the energetic prerequisites of site-to-site coupling and thus into how allostery works.
Journal ArticleDOI
Molecular titration and ultrasensitivity in regulatory networks.
TL;DR: It is demonstrated that molecular titration can generate ultrasensitivity on timescales compatible with most cell-fate decisions, and it is suggested that dominant negatives are abundant in gene regulatory circuits and might be generating an ultrasensitive response in these networks.
Journal ArticleDOI
Unfoldomics of human diseases: linking protein intrinsic disorder with diseases
Vladimir N. Uversky,Vladimir N. Uversky,Christopher J. Oldfield,Uros Midic,Hongbo Xie,Bin Xue,Slobodan Vucetic,Lilia M. Iakoucheva,Zoran Obradovic,A. Keith Dunker +9 more
TL;DR: Unfoldomics of human diseases utilizes unrivaled bioinformatics and experimental techniques, paves the road for better understanding of human Diseases, their pathogenesis and molecular mechanisms, and helps develop new strategies for the analysis of disease-related proteins.
Journal ArticleDOI
Interconversion between two unrelated protein folds in the lymphotactin native state
Robbyn L. Tuinstra,Francis C. Peterson,Snjezana Kutlesa,E. Sonay Elgin,Michael A. Kron,Brian F. Volkman +5 more
TL;DR: The results demonstrate that the functional repertoire and regulation of a single naturally occurring amino acid sequence can be expanded by access to a set of highly dissimilar native-state structures.
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Histone structure and nucleosome stability
TL;DR: Recent findings on the structure of chromatin are reviewed that confirm previous interparticle interactions observed in crystal structures and influence DNA replication, transcription, repair and recombination.
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.