1cnp: Difference between revisions
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==Overview== | ==Overview== | ||
The S100 calcium-binding proteins are implicated as effectors in | 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 Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Akke, M.]] | [[Category: Akke, M.]] | ||
[[Category: Case, D | [[Category: Case, D A.]] | ||
[[Category: Chazin, W | [[Category: Chazin, W J.]] | ||
[[Category: Hidaka, H.]] | [[Category: Hidaka, H.]] | ||
[[Category: Macke, T | [[Category: Macke, T J.]] | ||
[[Category: Okazaki, K.]] | [[Category: Okazaki, K.]] | ||
[[Category: Potts, B | [[Category: Potts, B C.M.]] | ||
[[Category: Smith, J.]] | [[Category: Smith, J.]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
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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 Thu Feb 21 12:07:58 2008'' | ||
Revision as of 13:07, 21 February 2008
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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. Known structural/functional Sites: , , and . 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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