+検索条件
-Structure paper
タイトル | Allosteric mechanism of water-channel gating by Ca2+-calmodulin. |
---|---|
ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 20, Issue 9, Page 1085-1092, Year 2013 |
掲載日 | 2013年7月28日 |
![]() | Steve L Reichow / Daniel M Clemens / J Alfredo Freites / Karin L Németh-Cahalan / Matthias Heyden / Douglas J Tobias / James E Hall / Tamir Gonen / ![]() |
PubMed 要旨 | Calmodulin (CaM) is a universal regulatory protein that communicates the presence of calcium to its molecular targets and correspondingly modulates their function. This key signaling protein is ...Calmodulin (CaM) is a universal regulatory protein that communicates the presence of calcium to its molecular targets and correspondingly modulates their function. This key signaling protein is important for controlling the activity of hundreds of membrane channels and transporters. However, understanding of the structural mechanisms driving CaM regulation of full-length membrane proteins has remained elusive. In this study, we determined the pseudoatomic structure of full-length mammalian aquaporin-0 (AQP0, Bos taurus) in complex with CaM, using EM to elucidate how this signaling protein modulates water-channel function. Molecular dynamics and functional mutation studies reveal how CaM binding inhibits AQP0 water permeability by allosterically closing the cytoplasmic gate of AQP0. Our mechanistic model provides new insight, only possible in the context of the fully assembled channel, into how CaM regulates multimeric channels by facilitating cooperativity between adjacent subunits. |
![]() | ![]() ![]() ![]() |
手法 | EM (単粒子) |
解像度 | 25.0 Å |
構造データ | |
化合物 | ![]() ChemComp-CA: |
由来 |
|
![]() | TRANSPORT PROTEIN/CALCIUM BINDING / calcium regulation / water channel / membrane protein complex / TRANSPORT PROTEIN-CALCIUM BINDING complex |