1IH5

CRYSTAL STRUCTURE OF AQUAPORIN-1

「1HW0」から置き換えられました

1IH5 の概要

• エントリーDOI: 10.2210/pdb1ih5/pdb
• 分子名称: AQUAPORIN-1 (1 entity in total)
• 機能のキーワード: membrane protein, water channel, two-dimensional crystal
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P29972
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28549.91

構造登録者

Ren, G.,Reddy, V.S.,Cheng, A.,Melnyk, P.,Mitra, A.K. (登録日: 2001-04-18, 公開日: 2001-04-25, 最終更新日: 2024-02-07)

主引用文献

Ren, G.,Reddy, V.S.,Cheng, A.,Melnyk, P.,Mitra, A.K.
Visualization of a water-selective pore by electron crystallography in vitreous ice.
Proc.Natl.Acad.Sci.USA, 98:1398-1403, 2001

PubMed Abstract: 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.

PubMed: 11171962
DOI: 10.1073/pnas.041489198

実験手法

ELECTRON CRYSTALLOGRAPHY (3.7 Å)