1cnp: Difference between revisions

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[[Image:1cnp.gif|left|200px]]
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{{STRUCTURE_1cnp|  PDB=1cnp  |  SCENE=  }}  
{{STRUCTURE_1cnp|  PDB=1cnp  |  SCENE=  }}  


'''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===




==Overview==
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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.
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{{ABSTRACT_PUBMED_7552751}}


==About this Structure==
==About this Structure==
1CNP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA].  
1CNP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA].  


==Reference==
==Reference==
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[[Category: Ef-hand]]
[[Category: Ef-hand]]
[[Category: S-100 protein]]
[[Category: S-100 protein]]
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