1dyk

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(New page: 200px<br /><applet load="1dyk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dyk, resolution 2.00&Aring;" /> '''LAMININ ALPHA 2 CHAI...)
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[[Image:1dyk.gif|left|200px]]<br /><applet load="1dyk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dyk, resolution 2.00&Aring;" />
 
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'''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR'''<br />
 
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==Overview==
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==Laminin alpha 2 chain LG4-5 domain pair==
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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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<StructureSection load='1dyk' size='340' side='right'caption='[[1dyk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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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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<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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==About this Structure==
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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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1DYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=1DYK OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10747011 10747011]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1dyk" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Hohenester, E.]]
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[[Category: Talts, J.F.]]
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[[Category: Timple, R.]]
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[[Category: Tisi, D.]]
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[[Category: CA]]
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[[Category: laminin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:41:05 2007''
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==See Also==
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*[[Laminin|Laminin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Hohenester E]]
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[[Category: Talts JF]]
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[[Category: Timple R]]
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[[Category: Tisi D]]

Current revision

Laminin alpha 2 chain LG4-5 domain pair

PDB ID 1dyk

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