2y38
From Proteopedia
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| - | [[Image:2y38.png|left|200px]] | ||
| - | + | ==LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT== | |
| + | <StructureSection load='2y38' size='340' side='right'caption='[[2y38]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2y38]] 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=2Y38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y38 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y38 OCA], [https://pdbe.org/2y38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y38 RCSB], [https://www.ebi.ac.uk/pdbsum/2y38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y38 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LAMA5_MOUSE LAMA5_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. Alpha-5 may be the major laminin alpha chain of adult epithelial and/or endothelial basal laminae. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The polymerization of laminin into a cell-associated network-a key step in basement membrane assembly-is mediated by the laminin amino-terminal (LN) domains at the tips of the three short arms of the laminin alphabetagamma-heterotrimer. The crystal structure of a laminin alpha5LN-LE1-2 fragment shows that the LN domain is a beta-jelly roll with several elaborate insertions that is attached like a flower head to the stalk-like laminin-type epidermal growth factor-like tandem. A surface loop that is strictly conserved in the LN domains of all alpha-short arms is required for stable ternary association with the beta- and gamma-short arms in the laminin network. | ||
| - | + | Determinants of laminin polymerization revealed by the structure of the alpha5 chain amino-terminal region.,Hussain SA, Carafoli F, Hohenester E EMBO Rep. 2011 Feb 11. PMID:21311558<ref>PMID:21311558</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2y38" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Laminin|Laminin]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Carafoli | + | [[Category: Carafoli F]] |
| - | [[Category: Hohenester | + | [[Category: Hohenester E]] |
| - | [[Category: Hussain | + | [[Category: Hussain SA]] |
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Current revision
LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT
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