Structural highlights
Function
[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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hussain SA, Carafoli F, Hohenester E. Determinants of laminin polymerization revealed by the structure of the alpha5 chain amino-terminal region. EMBO Rep. 2011 Feb 11. PMID:21311558 doi:10.1038/embor.2011.3
