+検索条件
-Structure paper
タイトル | Structural determinants of water permeation through aquaporin-1. |
---|---|
ジャーナル・号・ページ | Nature, Vol. 407, Issue 6804, Page 599-605, Year 2000 |
掲載日 | 2000年10月5日 |
著者 | K Murata / K Mitsuoka / T Hirai / T Walz / P Agre / J B Heymann / A Engel / Y Fujiyoshi / |
PubMed 要旨 | Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron ...Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons. |
リンク | Nature / PubMed:11034202 |
手法 | EM (電子線結晶学) |
解像度 | 3.8 Å |
構造データ | PDB-1fqy: |
由来 |
|
キーワード | MEMBRANE PROTEIN / WATER CHANNEL / TWO-DIMENSIONAL CRYSTAL |