1sra
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(New page: 200px<br /> <applet load="1sra" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sra, resolution 2.0Å" /> '''STRUCTURE OF A NOVEL...)
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Revision as of 17:10, 12 November 2007
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STRUCTURE OF A NOVEL EXTRACELLULAR CA2+-BINDING MODULE IN BM-40(SLASH)SPARC(SLASH)OSTEONECTIN
Overview
The EF-hand is a highly conserved Ca(2+)-binding motif found in many, cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure, at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair., The two EF-hands interact canonically but their detailed structures are, unusual. In the first EF-hand a one-residue insertion is accommodated by a, cis-peptide bond and by substituting a carboxylate by a peptide carbonyl, as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond., The EF-hand pair interacts tightly with an amphiphilic amino-terminal, helix, reminiscent of target peptide binding by calmodulin. The present, structure defines a novel protein module occurring in several other, extracellular proteins.
About this Structure
1SRA is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a novel extracellular Ca(2+)-binding module in BM-40., Hohenester E, Maurer P, Hohenadl C, Timpl R, Jansonius JN, Engel J, Nat Struct Biol. 1996 Jan;3(1):67-73. PMID:8548457
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