1dyk

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[[Image:1dyk.png|left|200px]]
 
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==Laminin alpha 2 chain LG4-5 domain pair==
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The line below this paragraph, containing "STRUCTURE_1dyk", creates the "Structure Box" on the page.
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<StructureSection load='1dyk' size='340' side='right'caption='[[1dyk]], [[Resolution|resolution]] 2.00&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'>[[1dyk]] 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=1DYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DYK 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&#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></td></tr>
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{{STRUCTURE_1dyk| PDB=1dyk | 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=1dyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyk OCA], [https://pdbe.org/1dyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dyk RCSB], [https://www.ebi.ac.uk/pdbsum/1dyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dyk 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/dy/1dyk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1dyk 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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The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The C-terminus of the laminin alpha chain contains a tandem of five laminin G-like (LG) domains. We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110 degrees rotation about an axis passing near the domain termini. An extended N-terminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to construct a model of the laminin LG1-LG5 tandem and interpret missense mutations underlying protein S deficiency.
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===LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR===
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Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin.,Tisi D, Talts JF, Timpl R, Hohenester E EMBO J. 2000 Apr 3;19(7):1432-40. PMID:10747011<ref>PMID:10747011</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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<div class="pdbe-citations 1dyk" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10747011}}, adds the Publication Abstract to the page
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*[[Laminin|Laminin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10747011 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10747011}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1dyk]] 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=1DYK OCA].
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==Reference==
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<ref group="xtra">PMID:10747011</ref><ref group="xtra">PMID:10619025</ref><ref group="xtra">PMID:9598981</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Hohenester, E.]]
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[[Category: Hohenester E]]
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[[Category: Talts, J F.]]
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[[Category: Talts JF]]
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[[Category: Timple, R.]]
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[[Category: Timple R]]
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[[Category: Tisi, D.]]
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[[Category: Tisi D]]
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[[Category: Laminin]]
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[[Category: Metal binding protein]]
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Current revision

Laminin alpha 2 chain LG4-5 domain pair

PDB ID 1dyk

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