1sra

<table><tr><td colspan='2'>[[1sra]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SRA FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HUMAN BM-40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sra OCA], [http://pdbe.org/1sra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sra RCSB], [http://www.ebi.ac.uk/pdbsum/1sra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sra ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SPRC_HUMAN SPRC_HUMAN]] Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.

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== 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<ref>PMID:8548457</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Engel, J]]

[[Category: Hohenadl, C]]

[[Category: Hohenester, E]]

[[Category: Jansonius, J N]]

[[Category: Maurer, P]]

[[Category: Timpl, R]]

[[Category: Extracellular matrix protein]]