2y38
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y38 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y38 RCSB], [http://www.ebi.ac.uk/pdbsum/2y38 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y38 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y38 RCSB], [http://www.ebi.ac.uk/pdbsum/2y38 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 03:22, 25 December 2014
LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT
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