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3m7p
From Proteopedia
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| - | [[Image:3m7p.png|left|200px]] | ||
| - | + | ==Fibronectin fragment== | |
| + | <StructureSection load='3m7p' size='340' side='right'caption='[[3m7p]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3m7p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3M7P FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3m7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7p OCA], [http://pdbe.org/3m7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m7p RCSB], [http://www.ebi.ac.uk/pdbsum/3m7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/3m7p_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3m7p ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fibronectin is a modular extracellular matrix protein involved in cell adhesion, cell motility, wound healing, and maintenance of cell morphology. It is composed of multiple repeats of three distinct modules: F(I), F(II), and F(III). Various combinations of these modules create fragments able to interact with different constituents of the extracellular matrix. Here, we present the 2.5-A resolution crystal structure of its 45-kDa gelatin-binding domain (GBD; 6F(I)-1F(II)-2F(II)-7F(I)-8F(I)-9F(I)), which also corresponds to the C-terminal half of the migration stimulating factor, a Fn splice variant expressed in human breast cancers. GBD forms a very compact zinc-mediated homodimer, in stark contrast with previous structures of fibronectin fragments. Most remarkably, 8F(I) no longer adopts the canonical F(I) fold but is composed of two long strands that associate with 7F(I) and 9F(I) into a large beta-sheet superdomain. Binding studies in solution confirmed that Zn induces conformational rearrangements and causes loss of binding of Fn-GBD to high-affinity collagen peptides. These data suggest the Zn may play a regulatory role for the cellular functions of fibronectin. | ||
| - | + | Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding.,Graille M, Pagano M, Rose T, Ravaux MR, van Tilbeurgh H Structure. 2010 Jun 9;18(6):710-8. PMID:20541508<ref>PMID:20541508</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3m7p" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
*[[Fibronectin|Fibronectin]] | *[[Fibronectin|Fibronectin]] | ||
| - | + | *[[Fibronectin 3D structures|Fibronectin 3D structures]] | |
| - | == | + | == References == |
| - | < | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Graille, M | + | </StructureSection> |
| - | [[Category: Pagano, M | + | [[Category: Human]] |
| - | [[Category: Ravaux, M Reboud | + | [[Category: Large Structures]] |
| - | [[Category: Rose, T | + | [[Category: Graille, M]] |
| - | [[Category: Tilbeurgh, H van | + | [[Category: Pagano, M]] |
| + | [[Category: Ravaux, M Reboud]] | ||
| + | [[Category: Rose, T]] | ||
| + | [[Category: Tilbeurgh, H van]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Conformational change]] | [[Category: Conformational change]] | ||
Current revision
Fibronectin fragment
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