1bmo
From Proteopedia
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|PDB= 1bmo |SIZE=350|CAPTION= <scene name='initialview01'>1bmo</scene>, resolution 3.10Å | |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> | |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> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmo OCA], [http://www.ebi.ac.uk/pdbsum/1bmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bmo RCSB]</span> | ||
}} | }} | ||
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[[Category: Maurer, P.]] | [[Category: Maurer, P.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
| - | [[Category: CA]] | ||
[[Category: anti-adhesive protein]] | [[Category: anti-adhesive protein]] | ||
[[Category: extracellular module]] | [[Category: extracellular module]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:04:05 2008'' |
Revision as of 16:04, 30 March 2008
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| , resolution 3.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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