1cnp: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [http://www.ebi.ac.uk/pdbsum/1cnp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB]</span> | |||
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[[Category: s-100 protein]] | [[Category: s-100 protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:05 2008'' | ||
Revision as of 19:25, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES
OverviewOverview
The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.
About this StructureAbout this Structure
1CNP is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins., Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ, Nat Struct Biol. 1995 Sep;2(9):790-6. PMID:7552751
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