1FQY

STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY

1FQY の概要

• エントリーDOI: 10.2210/pdb1fqy/pdb
• 分子名称: AQUAPORIN-1 (1 entity in total)
• 機能のキーワード: water channel, two-dimensional crystal, membrane 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: 28549.91

構造登録者

Murata, K.,Mitsuoka, K.,Hirai, T.,Walz, T.,Agre, P.,Heymann, J.B.,Engel, A.,Fujiyoshi, Y. (登録日: 2000-09-07, 公開日: 2000-10-18, 最終更新日: 2024-04-17)

主引用文献

Murata, K.,Mitsuoka, K.,Hirai, T.,Walz, T.,Agre, P.,Heymann, J.B.,Engel, A.,Fujiyoshi, Y.
Structural determinants of water permeation through aquaporin-1.
Nature, 407:599-605, 2000

PubMed Abstract: Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons.

PubMed: 11034202
DOI: 10.1038/35036519

実験手法

ELECTRON CRYSTALLOGRAPHY (3.8 Å)