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1cnp

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[[Image:1cnp.gif|left|200px]]
[[Image:1cnp.gif|left|200px]]
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{{Structure
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|SITE= <scene name='pdbsite=LO1:Ion+Binding+Site'>LO1</scene>, <scene name='pdbsite=LO2:Ion+Binding+Site'>LO2</scene>, <scene name='pdbsite=LO3:Ion+Binding+Site'>LO3</scene> and <scene name='pdbsite=LO4:Ion+Binding+Site'>LO4</scene>
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{{STRUCTURE_1cnp| PDB=1cnp | SCENE= }}
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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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'''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.]]
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[[Category: calcium-binding protein]]
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[[Category: Calcium-binding protein]]
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[[Category: ef-hand]]
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[[Category: Ef-hand]]
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[[Category: s-100 protein]]
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[[Category: S-100 protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:55:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:05 2008''
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Revision as of 09:55, 2 May 2008

Image:1cnp.gif

Template:STRUCTURE 1cnp

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

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