2wjs

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[[Image:2wjs.png|left|200px]]
 
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{{STRUCTURE_2wjs| PDB=2wjs | SCENE= }}
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==Crystal structure of the LG1-3 region of the laminin alpha2 chain==
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<StructureSection load='2wjs' size='340' side='right'caption='[[2wjs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2wjs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WJS FirstGlance]. <br>
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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]] 2.8&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wjs OCA], [https://pdbe.org/2wjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wjs RCSB], [https://www.ebi.ac.uk/pdbsum/2wjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wjs ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/LAMA2_MOUSE LAMA2_MOUSE] Note=Defects in Lama2 are a cause of murine muscular dystrophy (dy2J).
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== Function ==
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[https://www.uniprot.org/uniprot/LAMA2_MOUSE LAMA2_MOUSE] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
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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/wj/2wjs_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=2wjs 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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Laminins are large heterotrimeric glycoproteins with many essential functions in basement membrane assembly and function. Cell adhesion to laminins is mediated by a tandem of five laminin G-like (LG) domains at the C terminus of the alpha chain. Integrin binding requires an intact LG1-3 region, as well as contributions from the coiled coil formed by the alpha, beta, and gamma chains. We have determined the crystal structure at 2.8-A resolution of the LG1-3 region of the laminin alpha2 chain (alpha 2LG1-3). The three LG domains adopt typical beta-sandwich folds, with canonical calcium binding sites in LG1 and LG2. LG2 and LG3 interact through a substantial interface, but LG1 is completely dissociated from the LG2-3 pair. We suggest that the missing gamma chain tail may be required to stabilize the interaction between LG1 and LG2-3 in the biologically active conformation. A global analysis of N-linked glycosylation sites shows that the beta-sandwich faces of LG1 are free of carbohydrate modifications in all five laminin alpha chains, suggesting that these surfaces may harbor the integrin binding site. The alpha 2LG1-3 structure provides the first atomic view of the integrin binding region of laminins.
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===CRYSTAL STRUCTURE OF THE LG1-3 REGION OF THE LAMININ ALPHA2 CHAIN===
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Crystal structure of the LG1-3 region of the laminin alpha2 chain.,Carafoli F, Clout NJ, Hohenester E J Biol Chem. 2009 Aug 21;284(34):22786-92. Epub 2009 Jun 24. PMID:19553699<ref>PMID:19553699</ref>
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{{ABSTRACT_PUBMED_19553699}}
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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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==About this Structure==
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<div class="pdbe-citations 2wjs" style="background-color:#fffaf0;"></div>
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[[2wjs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WJS OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:019553699</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Carafoli, F.]]
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[[Category: Carafoli F]]
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[[Category: Clout, N J.]]
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[[Category: Clout NJ]]
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[[Category: Hohenester, E.]]
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[[Category: Hohenester E]]
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[[Category: Basement membrane]]
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[[Category: Cell adhesion]]
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[[Category: Disulfide bond]]
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[[Category: Extracellular matrix]]
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[[Category: Glycoprotein]]
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[[Category: Integrin]]
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[[Category: Laminin egf-like domain]]
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[[Category: Laminin g-like domain]]
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[[Category: Secreted]]
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Current revision

Crystal structure of the LG1-3 region of the laminin alpha2 chain

PDB ID 2wjs

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