5MC9

Crystal structure of the heterotrimeric integrin-binding region of laminin-111

5MC9 の概要

• エントリーDOI: 10.2210/pdb5mc9/pdb
• 分子名称: Laminin subunit alpha-1, Laminin subunit beta-1, Laminin subunit gamma-1, ... (5 entities in total)
• 機能のキーワード: extracellular matrix, cell adhesion, coiled coil, laminin g-like domain
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Secreted, extracellular space, extracellular matrix, basement membrane: P19137 P02469 P02468
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 83161.69

構造登録者

Pulido, D.,Hohenester, E. (登録日: 2016-11-09, 公開日: 2017-02-08, 最終更新日: 2024-10-16)

主引用文献

Pulido, D.,Hussain, S.A.,Hohenester, E.
Crystal Structure of the Heterotrimeric Integrin-Binding Region of Laminin-111.
Structure, 25:530-535, 2017

PubMed Abstract: Laminins are cell-adhesive glycoproteins that are essential for basement membrane assembly and function. Integrins are important laminin receptors, but their binding site on the heterotrimeric laminins is poorly defined structurally. We report the crystal structure at 2.13 Å resolution of a minimal integrin-binding fragment of mouse laminin-111, consisting of ∼50 residues of α1β1γ1 coiled coil and the first three laminin G-like (LG) domains of the α1 chain. The LG domains adopt a triangular arrangement, with the C terminus of the coiled coil situated between LG1 and LG2. The critical integrin-binding glutamic acid residue in the γ1 chain tail is surface exposed and predicted to bind to the metal ion-dependent adhesion site in the integrin β1 subunit. Additional contacts to the integrin are likely to be made by the LG1 and LG2 surfaces adjacent to the γ1 chain tail, which are notably conserved and free of obstructing glycans.

PubMed: 28132784
DOI: 10.1016/j.str.2017.01.002

実験手法

X-RAY DIFFRACTION (2.13 Å)