1bmo: Difference between revisions
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[[Image:1bmo.gif|left|200px]] | [[Image:1bmo.gif|left|200px]] | ||
'''BM-40, FS/EC DOMAIN PAIR''' | {{Structure | ||
|PDB= 1bmo |SIZE=350|CAPTION= <scene name='initialview01'>1bmo</scene>, resolution 3.10Å | |||
|SITE= <scene name='pdbsite=EF1:Ef-Hand+Ca+Binding+Site+1'>EF1</scene> and <scene name='pdbsite=EF2:Ef-Hand+Ca+Binding+Site+2'>EF2</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''BM-40, FS/EC DOMAIN PAIR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BMO is a [ | 1BMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMO OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9233787 9233787] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:13:02 2008'' | ||
Revision as of 08:13, 20 March 2008
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| 1bmo, resolution 3.10Å | |||||||||||||
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| Sites: | EF1 and EF2 | ||||||||||||
| Ligands: | CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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