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1bmo

From Proteopedia

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{{Seed}}
 
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[[Image:1bmo.png|left|200px]]
 
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==BM-40, FS/EC DOMAIN PAIR==
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The line below this paragraph, containing "STRUCTURE_1bmo", creates the "Structure Box" on the page.
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<StructureSection load='1bmo' size='340' side='right'caption='[[1bmo]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bmo]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1bmo| PDB=1bmo | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmo OCA], [https://pdbe.org/1bmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bmo RCSB], [https://www.ebi.ac.uk/pdbsum/1bmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bmo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPRC_HUMAN SPRC_HUMAN] Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/1bmo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bmo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===BM-40, FS/EC DOMAIN PAIR===
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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<ref>PMID:9233787</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_9233787}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1bmo" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9233787 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9233787}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1BMO is a 2 chains structure of sequences 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].
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==Reference==
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<ref group="xtra">PMID:9233787</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hohenester, E.]]
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[[Category: Large Structures]]
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[[Category: Maurer, P.]]
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[[Category: Hohenester E]]
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[[Category: Timpl, R.]]
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[[Category: Maurer P]]
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[[Category: Anti-adhesive protein]]
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[[Category: Timpl R]]
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[[Category: Extracellular module]]
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[[Category: Glycoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:13:58 2009''
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Current revision

BM-40, FS/EC DOMAIN PAIR

PDB ID 1bmo

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