This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1sra
From Proteopedia
|
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
Page seeded by OCA on Mon Nov 12 19:17:10 2007
