1BMO

BM-40, FS/EC DOMAIN PAIR

Summary for 1BMO

• Entry DOI: 10.2210/pdb1bmo/pdb
• Descriptor: BM-40, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION (3 entities in total)
• Functional Keywords: extracellular module, glycoprotein, anti-adhesive protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 55232.98

Authors

Hohenester, E.,Maurer, P.,Timpl, R. (deposition date: 1997-03-25, release date: 1997-10-15, Last modification date: 2024-10-30)

Primary citation

Hohenester, E.,Maurer, P.,Timpl, R.
Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40.
EMBO J., 16:3778-3786, 1997

PubMed Abstract: 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.

PubMed: 9233787
DOI: 10.1093/emboj/16.13.3778

Experimental method

X-RAY DIFFRACTION (3.1 Å)