| Literature DB >> 7552751 |
B C Potts1, J Smith, M Akke, T J Macke, K Okazaki, H Hidaka, D A Case, W J Chazin.
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.Entities:
Mesh：
Substances：
Year: 1995 PMID： 7552751 DOI： 10.1038/nsb0995-790
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368