Structural determinants of water permeation through aquaporin-1

被引：1384

作者：

Murata, K

Mitsuoka, K

Hirai, T

Walz, T

Agre, P

Heymann, JB

Engel, A

Fujiyoshi, Y ^{[1
]}

机构：

[1] Kyoto Univ, Fac Sci, Dept Biophys, Sakyo Ku, Kyoto 6068502, Japan

[2] Natl Inst Physiol Sci, Okazaki, Aichi 4448585, Japan

[3] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

[4] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA

[5] Johns Hopkins Univ, Sch Med, Dept Med, Baltimore, MD 21205 USA

[6] Univ Basel, Bioctr, ME Muller Inst Microscopy, CH-4056 Basel, Switzerland

来源：

NATURE | 2000年 / 407卷 / 6804期

关键词：

D O I：

10.1038/35036519

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 3.8 Angstrom 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 Angstrom 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.

引用

页码：599 / 605

页数：7

共 47 条

[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].