2y38

LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT

spinqualitylabelsall models 2y38, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y38 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: NAG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laminin

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