4CSK

human Aquaporin

4CSK の概要

• エントリーDOI: 10.2210/pdb4csk/pdb
• 分子名称: AQUAPORIN-1 (2 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : P29972
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31165.70

構造登録者

Ruiz-Carrillo, D.,To-Yiu-Ying, J.,Darwis, D.,Soon, C.H.,Cornvik, T.,Torres, J.,Lescar, J. (登録日: 2014-03-08, 公開日: 2014-12-24, 最終更新日: 2023-12-20)

主引用文献

Ruiz Carrillo, D.,To Yiu Ying, J.,Darwis, D.,Soon, C.H.,Cornvik, T.,Torres, J.,Lescar, J.
Crystallization and Preliminary Crystallographic Analysis of Human Aquaporin 1 at a Resolution of 3.28 A.
Acta Crystallogr.,Sect.F, 70:1657-, 2014

PubMed Abstract: Aquaporin water channels (AQPs) are found in almost every organism from humans to bacteria. In humans, 13 classes of AQPs control water and glycerol homeostasis. Knockout studies have suggested that modulating the activity of AQPs could be beneficial for the treatment of several pathologies. In particular, aquaporin 1 is a key factor in cell migration and angiogenesis, and constitutes a possible target for anticancer compounds and also for the treatment of glaucoma. Here, a preliminary crystallographic analysis at 3.28 Å resolution of crystals of human aquaporin 1 (hAQP1) obtained from protein expressed in Sf9 insect cells is reported. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 89.28, c = 174.9 Å, and contained one monomer per asymmetric unit. The hAQP1 biological tetramer is generated via the crystallographic fourfold axis. This work extends previous electron crystallographic studies that used material extracted from human red blood cells, in which the resolution was limited to approximately 3.8 Å. It will inform efforts to improve lattice contacts and the diffraction limit for the future structure-based discovery of specific hAQP1 inhibitors.

PubMed: 25484221
DOI: 10.1107/S2053230X14024558

実験手法

X-RAY DIFFRACTION (3.28 Å)