title: Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region.
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.
authors.affiliation: Department of Life Sciences, Biophysics Section, Blackett Laboratory, Prince Consort Road, Imperial College London, London SW7 2AZ, UK.
authors.forename: Sadaf-Ahmahni
authors.initials: SA
authors.lastname: Hussain
authors.forename: Federico
authors.initials: F
authors.lastname: Carafoli
authors.forename: Erhard
authors.initials: E
authors.lastname: Hohenester
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001485:Basement Membrane / Q000737:chemistry; D001665:Binding Sites; D007797:Laminin / Q000737:chemistry* / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D058105:Polymerization; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D007797:Laminin; C121346:laminin 1