2Y38

LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT

2Y38 の概要

• エントリーDOI: 10.2210/pdb2y38/pdb
• 分子名称: LAMININ SUBUNIT ALPHA-5, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: structural protein, cell adhesion, basement membrane
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45971.29

構造登録者

Hussain, S.A.,Carafoli, F.,Hohenester, E. (登録日: 2010-12-19, 公開日: 2011-02-23, 最終更新日: 2024-11-20)

主引用文献

Hussain, S.A.,Carafoli, F.,Hohenester, E.
Determinants of Laminin Polymerisation Revealed by the Crystal Structure of the Alpha5 Chain Amino-Terminal Region
Embo Rep., 12:276-, 2011

PubMed 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.

PubMed: 21311558
DOI: 10.1038/EMBOR.2011.3

実験手法

X-RAY DIFFRACTION (2.9 Å)