1bmo: Difference between revisions

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[[Image:1bmo.gif|left|200px]]
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[[Image:1bmo.png|left|200px]]


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{{STRUCTURE_1bmo|  PDB=1bmo  |  SCENE=  }}  
{{STRUCTURE_1bmo|  PDB=1bmo  |  SCENE=  }}  


'''BM-40, FS/EC DOMAIN PAIR'''
===BM-40, FS/EC DOMAIN PAIR===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9233787}}


==About this Structure==
==About this Structure==
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[[Category: Extracellular module]]
[[Category: Extracellular module]]
[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
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Revision as of 16:23, 30 June 2008

File:1bmo.png

Template:STRUCTURE 1bmo

BM-40, FS/EC DOMAIN PAIR

Template:ABSTRACT PUBMED 9233787

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

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