水通道蛋白门控

Aquaporin gating.

作者信息

Hedfalk Kristina, Törnroth-Horsefield Susanna, Nyblom Maria, Johanson Urban, Kjellbom Per, Neutze Richard

机构信息

Chalmers University of Technology, Department of Chemistry and Bioscience, SE-405 30 Göteborg, Sweden.

出版信息

Curr Opin Struct Biol. 2006 Aug;16(4):447-56. doi: 10.1016/j.sbi.2006.06.009. Epub 2006 Jul 11.

DOI:10.1016/j.sbi.2006.06.009

PMID:16837191

Abstract

An acceleration in the rate at which new aquaporin structures are determined means that structural models are now available for mammalian AQP0, AQP1, AQP2 and AQP4, bacterial GlpF, AqpM and AQPZ, and the plant SoPIP2;1. With an apparent consensus emerging concerning the mechanism of selective water transport and proton extrusion, emphasis has shifted towards the issues of substrate selectivity and the mechanisms of aquaporin regulation. In particular, recently determined structures of plant SoPIP2;1, sheep and bovine AQP0, and Escherichia coli AQPZ provide new insights into the underlying structural mechanisms by which water transport rates are regulated in diverse organisms. From these results, two distinct pictures of 'capping' and 'pinching' have emerged to describe aquaporin gating.

摘要

新水通道蛋白结构确定速度的加快意味着现在已有哺乳动物水通道蛋白0（AQP0）、水通道蛋白1（AQP1）、水通道蛋白2（AQP2）和水通道蛋白4（AQP4）、细菌甘油通透蛋白（GlpF）、水通道蛋白M（AqpM）和水通道蛋白Z（AQPZ）以及植物质膜内在蛋白2;1（SoPIP2;1）的结构模型。随着关于选择性水运输和质子排出机制的明显共识的出现，重点已转向底物选择性问题和水通道蛋白调节机制。特别是，最近确定的植物SoPIP2;1、绵羊和牛AQP0以及大肠杆菌AQPZ的结构为不同生物体中调节水运输速率的潜在结构机制提供了新见解。从这些结果中，出现了两种不同的“封端”和“挤压”图景来描述水通道蛋白门控。