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Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region

DOI: 10.1038/embor.2011.3 DOI Help
PMID: 21311558 PMID Help

Authors: Sadaf-ahmahni Hussain (Imperial Collge London) , Federico Carafoli (Imperial College London) , Erhard Hohenester (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Embo Reports

State: Published (Approved)
Published: February 2011

Open Access Open Access

Abstract: 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 αβγ-heterotrimer. The crystal structure of a laminin α5LN–LE1–2 fragment shows that the LN domain is a β-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 α-short arms is required for stable ternary association with the β- and γ-short arms in the laminin network.

Journal Keywords: Animals; Basement; Binding; Laminin; Mice; Models; Molecular; Polymerization; Protein; Quaternary; Protein; Tertiary

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography