期刊
BIOPHYSICAL JOURNAL
卷 96, 期 7, 页码 2572-2576出版社
CELL PRESS
DOI: 10.1016/j.bpj.2008.12.3927
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资金
- Consejo Nacional de Ciencia Tecnologia, Mexico
- National Institutes of Health [GM74637, GM68002]
- Direct For Mathematical & Physical Scien [0750175] Funding Source: National Science Foundation
- Division Of Chemistry [0750175] Funding Source: National Science Foundation
Understanding the mechanism of G-protein coupled receptors action is of major interest for drug design. The visual rhodopsin is the prototype structure for the family A of G-protein coupled receptors. Upon photoisomerization of the covalently bound retinal chromophore, visual rhodopsins undergo a large-scale conformational change that prepares the receptor for a productive interaction with the G-protein. The mechanism by which the local perturbation of the retinal cis-trans isomerization is transmitted throughout the protein is not well understood. The crystal structure of the visual rhodopsin from squid solved recently suggests that a chain of water molecules extending from the retinal toward the cytoplasmic side of the protein may play a role in the signal transduction from the all-trans retinal geometry to the activated receptor. As a first step toward understanding the role of water in rhodopsin function, we performed a molecular dynamics simulation of squid rhodopsin embedded in a hydrated bilayer of polyunsaturated lipid molecules. The simulation indicates that the water molecules present in the crystal structure participate in favorable interactions with side chains in the interhelical region and form a persistent hydrogen-bond network in connecting Y315 to W274 via D80.
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