1bmo: Difference between revisions
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'''BM-40, FS/EC DOMAIN PAIR''' | '''BM-40, FS/EC DOMAIN PAIR''' | ||
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[[Category: Maurer, P.]] | [[Category: Maurer, P.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: | [[Category: Anti-adhesive protein]] | ||
[[Category: | [[Category: Extracellular module]] | ||
[[Category: | [[Category: Glycoprotein]] | ||
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Revision as of 08:42, 2 May 2008
BM-40, FS/EC DOMAIN PAIR
Overview
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.
About this Structure
1BMO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40., Hohenester E, Maurer P, Timpl R, EMBO J. 1997 Jul 1;16(13):3778-86. PMID:9233787 Page seeded by OCA on Fri May 2 11:42:22 2008
