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Nat Struct Biol. 1995 Sep;2(9):790-6.

The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.

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  • 1Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA.

Erratum in

  • Nat Struct Biol 1995 Oct;2(10):912.

Abstract

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.

PMID:
7552751
[PubMed - indexed for MEDLINE]
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