2y38: Difference between revisions

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'''Unreleased structure'''


The entry 2y38 is ON HOLD
==LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT==
<StructureSection load='2y38' size='340' side='right'caption='[[2y38]], [[Resolution|resolution]] 2.90&Aring;' 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]] 2.9&#8491;</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.


Authors: Hussain, S.A., Carafoli, F., Hohenester, E.
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>


Description: Laminin alpha5 chain N-terminal fragment
From MEDLINE&reg;/PubMed&reg;, 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: Carafoli F]]
[[Category: Hohenester E]]
[[Category: Hussain SA]]
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