1PU4

Crystal structure of human vascular adhesion protein-1

1PU4 の概要

• エントリーDOI: 10.2210/pdb1pu4/pdb
• 分子名称: Membrane copper amine oxidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: amine oxidase, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type II membrane protein: Q16853
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 171047.75

構造登録者

Salminen, T.A.,Airenne, T.T. (登録日: 2003-06-24, 公開日: 2005-05-03, 最終更新日: 2023-08-16)

主引用文献

Airenne, T.T.,Nymalm, Y.,Kidron, H.,Smith, D.J.,Pihlavisto, M.,Salmi, M.,Jalkanen, S.,Johnson, M.S.,Salminen, T.A.
Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.
Protein Sci., 14:1964-1974, 2005

PubMed Abstract: The expression of human vascular adhesion protein-1 (hVAP-1) is induced at sites of inflammation where extravasation of lymphocytes from blood to the peripheral tissue occurs. We have solved the X-ray structure of hVAP-1, a human copper amine oxidase (CAO), which is distinguished from other CAOs in being membrane-bound. The dimer structure reveals some intriguing features that may have fundamental roles in the adhesive and enzymatic functions of hVAP-1, especially regarding the role of hVAP-1 in inflammation, lymphocyte attachment, and signaling. Firstly, Leu469 at the substrate channel may play a key role in controlling the substrate entry; depending on its conformation, it either blocks or gives access to the active site. Secondly, sugar units are clearly observed at two of the six predicted N-glycosylation sites. Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization. Thirdly, the existence of a solvent-exposed RGD motif at the entrance to each active site in hVAP-1 suggests that it may have a functional role.

PubMed: 16046623
DOI: 10.1110/ps.051438105

実験手法

X-RAY DIFFRACTION (3.2 Å)