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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Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2
Joshua N. Adkins,Kevin J. Lumb +1 more
TL;DR: The amino acid composition of the CDK inhibition domain of p57 does not exhibit such a striking deviation from the average values observed for proteins, implying that a general low level of hydrophobicity, rather than depletion or enrichment in specific amino acids, contributes to the intrinsic disorder of the excised p57 CDK inhibited domain.
Journal ArticleDOI
Role of intrinsically disordered protein regions/domains in transcriptional regulation.
TL;DR: There are reports showing that ID regions/domains commonly exist within proteins with modular structures such as transcription factors, and are often located in their transactivation domain, and it is important to find out their existence and functional roles in transcriptional regulations by transcription factors.
Journal ArticleDOI
Integrating folding kinetics and protein function: Biphasic kinetics and dual binding specificity in a WW domain
TL;DR: The hypothesis that lability with respect to conformations separated by an observable barrier as a requirement for function is incompatible with the ability of a protein to fold via single-exponential kinetics is led to.
Journal ArticleDOI
Estimating the prevalence of protein sequences adopting functional enzyme folds.
TL;DR: The prevalence of low-level function in four such experiments indicates that roughly one in 10 signature-consistent sequences forms a working domain, implying the overall prevalence of sequences performing a specific function by any domain-sized fold may be as low as 1 in 10(77), adding to the body of evidence that functional folds require highly extraordinary sequences.
Journal ArticleDOI
Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.
Alexander V. Fonin,April L. Darling,Irina M. Kuznetsova,Konstantin K. Turoverov,Konstantin K. Turoverov,Vladimir N. Uversky +5 more
TL;DR: This review represents a systematic analysis of the available literature data on the behaviour of IDPs/IDPRs in crowded environment and indicates that, based on their response to the presence of crowders, IDPs or intrinsically disordered protein regions can be grouped into three major categories, foldable, non-foldable, and unfoldable.
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.
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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.