1bmo: Difference between revisions

BM-40 (also known as SPARC or osteonectin) is an anti-adhesive secreted, glycoprotein involved in tissue remodelling. Apart from an acidic, N-terminal segment, BM-40 consists of a follistatin-like (FS) domain and, an EF-hand calcium-binding (EC) domain. Here we report the crystal, structure at 3.1 A resolution of the FS-EC domain pair of human BM-40. The, two distinct domains interact through a small interface that involves the, EF-hand pair of the EC domain. Residues implicated in cell binding, inhibition of cell spreading and disassembly of focal adhesions cluster on, one face of BM-40, opposite the binding epitope for collagens and the, N-linked carbohydrate. The elongated FS domain is structurally related to, serine protease inhibitors of the Kazal family. Notable differences are an, insertion into the inhibitory loop in BM-40 and a protruding N-terminal, beta-hairpin with striking similarities to epidermal growth factor. This, hairpin is likely to act as a rigid spacer in proteins containing tandemly, repeated FS domains, such as follistatin and agrin, and forms the, heparin-binding site in follistatin.

1BMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: EF1 and EF2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMO OCA].  

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