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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A tale of two citrullines--structural and functional aspects of myelin basic protein deimination in health and disease.
George Harauz,Abdiwahab A. Musse +1 more
TL;DR: The degree of deimination (or citrullination) of MBP is correlated with the severity of MS, and may represent a primary defect that precedes neurodegeneration due to autoimmune attack, which indicates that this modification plays major physiological roles in myelin assembly.
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Advances in vibrational spectroscopy as a sensitive probe of peptide and protein structure A critical review
Journal ArticleDOI
Archaic chaos: intrinsically disordered proteins in Archaea
Bin Xue,Robert W. Williams,Christopher J. Oldfield,A. K. Dunker,Vladimir N. Uversky,Vladimir N. Uversky +5 more
TL;DR: The analysis based on the disordered content and phylogenetic tree indicated diverse evolution of intrinsic disorder among various classes and species of Archaea.
Journal ArticleDOI
p57KIP2: “Kip”ing the Cell under Control
Ioannis S. Pateras,Kalliopi Apostolopoulou,Katerina Niforou,Athanassios Kotsinas,Vassilis G. Gorgoulis +4 more
TL;DR: A thorough analysis of data available on p57KIP2, in relation to p21CIP1/WAF1 and p27KIP1, on gene and protein structure, its transcriptional and translational regulation, and its role in human physiology and pathology, focusing on cancer development is reviewed.
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A simple model for polyproline II structure in unfolded states of alanine-based peptides.
Rohit V. Pappu,George D. Rose +1 more
TL;DR: The results are based on a detailed analysis of the potential energy landscape which determines the system's structural and thermodynamic preferences and find that the landscape for the experimentally studied seven‐residue alanine‐based peptide is dominated by fluctuations about two noncooperative structures: the left‐handed polyproline II helix and its symmetry mate.
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.