1a03: Difference between revisions
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Revision as of 15:38, 30 October 2007
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THE THREE-DIMENSIONAL STRUCTURE OF CA2+-BOUND CALCYCLIN: IMPLICATIONS FOR CA2+-SIGNAL TRANSDUCTION BY S100 PROTEINS, NMR, 20 STRUCTURES
OverviewOverview
BACKGROUND: Calcyclin is a member of the S100 subfamily of EF-hand, Ca(2+)-binding proteins. This protein has implied roles in the regulation, of cell growth and division, exhibits deregulated expression in, association with cell transformation, and is found in high abundance in, certain breast cancer cell lines. The novel homodimeric structural motif, first identified for apo calcyclin raised the possibility that S100, proteins recognize their targets in a manner that is distinctly different, from that of the prototypical EF-hand Ca2+ sensor, calmodulin. The NMR, solution structure of Ca(2+)-bound calcyclin has been determined in order, to identify Ca(2+)-induced structural changes and to obtain insights into, the mechanism of Ca(2+)-triggered target protein recognition. RESULTS: The, ... [(full description)]
About this StructureAbout this Structure
1A03 is a [Single protein] structure of sequence from [Oryctolagus cuniculus]. Structure known Active Sites: , L2 and LI. Full crystallographic information is available from [OCA].
ReferenceReference
The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins., Sastry M, Ketchem RR, Crescenzi O, Weber C, Lubienski MJ, Hidaka H, Chazin WJ, Structure. 1998 Feb 15;6(2):223-31. PMID:9519412
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