Structural Basis of the Ca2+ Dependent Association between S100C (S100A11) and its Target, the N-Terminal Part of Annexin I
Stéphane Réty,Dirk Osterloh,Jean Philippe Arié,Sébastien Tabaries,Joachim Seeman,Françoise Russo-Marie,Volker Gerke,Anita Lewit-Bentley +7 more
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TLDR
By solving the structure of a second annexin N terminus-S100 protein complex, this work confirmed a novel mode of interaction of S100 proteins with their target peptides; there is a one-to-one stoichiometry, where the dimeric structure of the S100 protein is, nevertheless, essential for complex formation.About:
This article is published in Structure.The article was published on 2000-02-01 and is currently open access. It has received 175 citations till now. The article focuses on the topics: Protein structure & Protein family.read more
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Journal ArticleDOI
Annexins: from structure to function.
Volker Gerke,Stephen E. Moss +1 more
TL;DR: Although annexins lack signal sequences for secretion, some members of the family have also been identified extracellularly where they can act as receptors for serum proteases on the endothelium as well as inhibitors of neutrophil migration and blood coagulation.
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S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles.
TL;DR: The variety of intracellular target proteins of S100 proteins and, in some cases, of a single S100 protein, and the cell specificity of expression of certain S100 members suggest that these proteins might have a role in the fine regulation of effector proteins and/or specific steps of signaling pathways/cellular functions.
Journal ArticleDOI
Annexins: linking Ca2+ signalling to membrane dynamics.
TL;DR: Eukaryotic cells contain various Ca2-effector proteins that mediate cellular responses to changes in intracellular Ca2+ levels, and a unique class of these proteins — annexins — can bind to certain membrane phospholipids in a Ca2+.
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S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature)
TL;DR: This work analyzed the structural variations, which are the basis of functional diversification, as well as the genomic organization of the S100 family in human and compared it with the S 100 repertoires in mouse and rat, and identified evolutionary related subgroups of S100 proteins within the three species.
Journal ArticleDOI
S100 proteins: structure, functions and pathology.
TL;DR: S100 proteins have received increasing attention due to their close association with several human diseases including cardiomyopathy, neurodegenerative disorders and cancer, and are considered having a potential as drug targets to improve therapies.
References
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Book ChapterDOI
Processing of X-ray diffraction data collected in oscillation mode
Zbyszek Otwinowski,Wladek Minor +1 more
TL;DR: The methods presented in the chapter have been applied to solve a large variety of problems, from inorganic molecules with 5 A unit cell to rotavirus of 700 A diameters crystallized in 700 × 1000 × 1400 A cell.
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PROCHECK: a program to check the stereochemical quality of protein structures
TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
Journal ArticleDOI
The CCP4 suite: programs for protein crystallography
TL;DR: The CCP4 (Collaborative Computational Project, number 4) program suite is a collection of programs and associated data and subroutine libraries which can be used for macromolecular structure determination by X-ray crystallography.
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.