1bmo

From Proteopedia

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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