Aquaporin gating.
Curr Opin Struct Biol
; 16(4): 447-56, 2006 Aug.
Article
en En
| MEDLINE
| ID: mdl-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.
Buscar en Google
Base de datos:
MEDLINE
Asunto principal:
Acuaporinas
Idioma:
En
Revista:
Curr Opin Struct Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2006
Tipo del documento:
Article