Title : Crystal structure of a pair of
follistatin-like and EF-hand calcium-binding
domains in
BM-40
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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycoprotein, , BM-40, -, -
- 1. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
- 0. BM-40, domains
- 0. follistatin, domains
- 2. follistatin, domain
- 5. BM-40, face
- 8. follistatin, domains
- 8. follistatin, site
- 8. proteins, domains
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):