1bmo
From Proteopedia
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==Overview== | ==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, .. | + | 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== | ==About this Structure== | ||
| - | 1BMO is a | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:43:47 2007'' |
Revision as of 11:38, 5 November 2007
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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 with CA as ligand. Structure known Active Sites: EF1 and EF2. 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
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