6O5E

Crystal structure of the Vitronectin hemopexin-like domain

6O5E の概要

• エントリーDOI: 10.2210/pdb6o5e/pdb
• 分子名称: Vitronectin, SODIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: integrin ligand, hemopexin-like domain, beta-propeller, serum protein, cell adhesion
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47454.54

構造登録者

Lechtenberg, B.C.,Shin, K.,Marassi, F.M. (登録日: 2019-03-01, 公開日: 2019-09-18, 最終更新日: 2024-10-30)

主引用文献

Shin, K.,Lechtenberg, B.C.,Fujimoto, L.M.,Yao, Y.,Bartra, S.S.,Plano, G.V.,Marassi, F.M.
Structure of human Vitronectin C-terminal domain and interaction withYersinia pestisouter membrane protein Ail.
Sci Adv, 5:eaax5068-eaax5068, 2019

PubMed Abstract: Vitronectin (Vn) is a major component of blood that controls many processes central to human biology. It is a drug target and a key factor in cell and tissue engineering applications, but despite long-standing efforts, little is known about the molecular basis for its functions. Here, we define the domain organization of Vn, report the crystal structure of its carboxyl-terminal domain, and show that it harbors the binding site for the outer membrane protein Ail, which recruits Vn to the bacterial cell surface to evade human host defenses. Vn forms a single four-bladed β/α-propeller that serves as a hub for multiple functions. The structure explains key features of native Vn and provides a blueprint for understanding and targeting this essential human protein.

PubMed: 31535027
DOI: 10.1126/sciadv.aax5068

実験手法

X-RAY DIFFRACTION (1.9 Å)