Summary for 1IH5
| Entry DOI | 10.2210/pdb1ih5/pdb |
| Descriptor | AQUAPORIN-1 (1 entity in total) |
| Functional Keywords | membrane protein, water channel, two-dimensional crystal |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Multi-pass membrane protein: P29972 |
| Total number of polymer chains | 1 |
| Total formula weight | 28549.91 |
| Authors | Ren, G.,Reddy, V.S.,Cheng, A.,Melnyk, P.,Mitra, A.K. (deposition date: 2001-04-18, release date: 2001-04-25, Last modification date: 2024-02-07) |
| Primary citation | 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 Cited by 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: 11171962DOI: 10.1073/pnas.041489198 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (3.7 Å) |
Structure validation
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