1bmo

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(New page: 200px<br /> <applet load="1bmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmo, resolution 3.10&Aring;" /> '''BM-40, FS/EC DOMAIN...)
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==About this Structure==
==About this Structure==
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1BMO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMO OCA]].
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1BMO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: EF1 and EF2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMO OCA]].
==Reference==
==Reference==
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[[Category: glycoprotein]]
[[Category: glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:47:59 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:05:44 2007''

Revision as of 10:01, 30 October 2007


1bmo, resolution 3.10Å

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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, ... [(full description)]

About this Structure

1BMO is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Sites: EF1 and EF2. 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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