Department of Life Sciences, Biophysics Section, Blackett Laboratory, Prince Consort Road, Imperial College London, London SW7 2AZ, UK.
EMBO Rep. 2011 Mar;12(3):276-82. doi: 10.1038/embor.2011.3. Epub 2011 Feb 11.
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.
层粘连蛋白在细胞相关网络中的聚合——基底膜组装的关键步骤——是由层粘连蛋白αβγ三聚体三个短臂末端的层粘连蛋白氨基端（LN）结构域介导的。层粘连蛋白α5LN-LE1-2 片段的晶体结构表明，LN 结构域是一个具有多个复杂插入物的β-发夹，类似于柄状层粘连蛋白型表皮生长因子样串联物的花头。在所有α-短臂的 LN 结构域中严格保守的表面环对于稳定的三元与层粘连蛋白网络中的β-和γ-短臂的缔合是必需的。
