A refined structure of human aquaporin-1

被引：112

作者：

de Groot, BL

Engel, A

Grubmüller, H

机构：

[1] Max Planck Inst Biophys Chem, Theoret Mol Biophys Grp, D-37077 Gottingen, Germany

[2] Univ Basel, Bioctr, ME Muller Inst Microscop Struct Biol, CH-4056 Basel, Switzerland

来源：

FEBS LETTERS | 2001年 / 504卷 / 03期

关键词：

protein structure; electron microscopy; water transport; water channel; membrane protein; glycerol transporter; aquaporin-1; GlpF;

D O I：

10.1016/S0014-5793(01)02743-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 Angstrom resolution and a multiple sequence alignment of the aquaporin superfamily. The crystallographic R and free R values (36.7% and 37.8%) for the refined structure are significantly lower than for previous models. Improved geometry and enhanced stability in molecular dynamics simulations demonstrate a significant improvement of the aquaporin-1 structure. Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：206 / 211

页数：6

共 36 条

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