1ih5
From Proteopedia
CRYSTAL STRUCTURE OF AQUAPORIN-1
Overview
The water-selective pathway through the aquaporin-1 membrane channel has been visualized by fitting an atomic model to a 3.7-A resolution three-dimensional density map. This map was determined by analyzing images and electron diffraction patterns of lipid-reconstituted two-dimensional crystals of aquaporin-1 preserved in vitrified buffer in the absence of any additive. The aqueous pathway is characterized by a size-selective pore that is approximately 4.0 +/- 0.5A in diameter, spans a length of approximately 18A, and bends by approximately 25 degrees as it traverses the bilayer. This narrow pore is connected by wide, funnel-shaped openings at the extracellular and cytoplasmic faces. The size-selective pore is outlined mostly by hydrophobic residues, resulting in a relatively inert pathway conducive to diffusion-limited water flow. The apex of the curved pore is close to the locations of the in-plane pseudo-2-fold symmetry axis that relates the N- and C-terminal halves and the conserved, functionally important N76 and N192 residues.
About this Structure
1IH5 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1hw0. Full crystallographic information is available from OCA.
Reference
Visualization of a water-selective pore by electron crystallography in vitreous ice., Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1398-403. Epub 2001 Jan 30. PMID:11171962 Page seeded by OCA on Fri May 2 19:59:38 2008
