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1sra
From Proteopedia
Revision as of 14:11, 29 September 2014 by OCA (Talk | contribs)
1sra is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Hohenester E, Maurer P, Hohenadl C, Timpl R, Jansonius JN, Engel J. Structure of a novel extracellular Ca(2+)-binding module in BM-40. Nat Struct Biol. 1996 Jan;3(1):67-73. PMID:8548457
