4AQS

Laminin beta1 LN-LE1-4 structure

4AQS の概要

• エントリーDOI: 10.2210/pdb4aqs/pdb
• 関連するPDBエントリー: 4AQT
• 分子名称: LAMININ SUBUNIT BETA-1, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix, basement membrane: P02469
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59816.00

構造登録者

Carafoli, F.,Hussain, S.,Hohenester, E. (登録日: 2012-04-19, 公開日: 2012-08-15, 最終更新日: 2024-10-23)

主引用文献

Carafoli, F.,Hussain, S.,Hohenester, E.
Crystal Structures of the Network-Forming Short-Arm Tips of the Laminin Beta1 and Gamma1 Chains.
Plos One, 7:42473-, 2012

PubMed Abstract: The heterotrimeric laminins are a defining component of basement membranes and essential for tissue formation and function in all animals. The three short arms of the cross-shaped laminin molecule are composed of one chain each and their tips mediate the formation of a polymeric network. The structural basis for laminin polymerisation is unknown. We have determined crystal structures of the short-arm tips of the mouse laminin β1 and γ1 chains, which are grossly similar to the previously determined structure of the corresponding α5 chain region. The short-arm tips consist of a laminin N-terminal (LN) domain that is attached like the head of a flower to a rod-like stem formed by tandem laminin-type epidermal growth factor-like (LE) domains. The LN domain is a β-sandwich with elaborate loop regions that differ between chains. The γ1 LN domain uniquely contains a calcium binding site. The LE domains have little regular structure and are stabilised by cysteines that are disulphide-linked 1-3, 2-4, 5-6 and 7-8 in all chains. The LN surface is not conserved across the α, β and γ chains, but within each chain subfamily there is a striking concentration of conserved residues on one face of the β-sandwich, while the opposite face invariably is shielded by glycans. We propose that the extensive conserved patches on the β and γ LN domains mediate the binding of these two chains to each other, and that the α chain LN domain subsequently binds to the composite β-γ surface. Mutations in the laminin β2 LN domain causing Pierson syndrome are likely to impair the folding of the β2 chain or its ability to form network interactions.

PubMed: 22860131
DOI: 10.1371/JOURNAL.PONE.0042473

実験手法

X-RAY DIFFRACTION (3.109 Å)