1cnp: Difference between revisions
New page: left|200px<br /> <applet load="1cnp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cnp" /> '''THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL ... |
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==About this Structure== | ==About this Structure== | ||
1CNP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]]. | 1CNP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]]. Structure known Active Sites: LO1, LO2, LO3 and LO4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: s-100 protein]] | [[Category: s-100 protein]] | ||
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Revision as of 09:20, 30 October 2007
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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]. Structure known Active Sites: LO1, LO2, LO3 and LO4. 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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