1cnp
From Proteopedia
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'''THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES''' | '''THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES''' | ||
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[[Category: Potts, B C.M.]] | [[Category: Potts, B C.M.]] | ||
[[Category: Smith, J.]] | [[Category: Smith, J.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding protein]] |
| - | [[Category: | + | [[Category: Ef-hand]] |
| - | [[Category: | + | [[Category: S-100 protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:55:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:55, 2 May 2008
THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES
Overview
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
1CNP is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 12:55:26 2008
