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 disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes
Amrita Mohan,William J. Sullivan,Predrag Radivojac,A. Keith Dunker,Vladimir N. Uversky,Vladimir N. Uversky +5 more
TL;DR: This study provides a bioinfomatics basis for the discovery and analysis of unfoldomes (the complement of intrinsically disordered proteins in a given proteome) of early-branching eukaryotes and provides new insights into the evolution of intrinsic disorder in the context of adapting to a parasitic lifestyle.
Journal ArticleDOI
A functionally required unfoldome from the plant kingdom: intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development.
Xiaolin Sun,Bin Xue,William T. Jones,Erik H. A. Rikkerink,A. Keith Dunker,Vladimir N. Uversky,Vladimir N. Uversky +6 more
TL;DR: It is demonstrated here that the GRAS proteins are intrinsically disordered, thus forming the first functionally required unfoldome in the plant kingdom, and a conceptual framework is proposed that guides future experimental approaches to understand structure–function relationships of the entire GRAS family.
Journal ArticleDOI
Conformation of a Group 2 Late Embryogenesis Abundant Protein from Soybean. Evidence of Poly (l-Proline)-type II Structure
TL;DR: The ability of the protein to remain in a highly extended conformation at low temperatures could constitute the basis of the functional role of GmDHN1 in the prevention of freezing, desiccation, ionic, or osmotic stress-related damage to macromolecular structures.
Journal ArticleDOI
Surface-decoration of microtubules by human tau.
Rachel Santarella,Georgios Skiniotis,Kenneth N. Goldie,Peter Tittmann,Heinz Gross,Eva Maria Mandelkow,Eckhard Mandelkow,Andreas Hoenger +7 more
TL;DR: The data suggest that tau retains most of its disordered structure even when bound to the microtubule surface, which suggests that it binds along, as well as across protofilaments.
Journal ArticleDOI
Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules.
Daniela Fischer,Marco D. Mukrasch,Jacek Biernat,Stefan Bibow,Martin Blackledge,Christian Griesinger,Eckhard Mandelkow,Markus Zweckstetter +7 more
TL;DR: Investigating the impact of phosphorylation on the conformational and binding properties of the repeat region of tau (K18) that is necessary for microtubule assembly and forms the core of paired helical filaments induces specific conformational changes that have a strong impact on its biological function and involvement in disease.
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.