A specific cholesterol binding site is established by the 2.8 Å structure of the human β(2)-adrenergic receptor in an alternate crystal form

The role of cholesterol in eukaryotic membrane protein function has been primarily attributed to an influence on membrane fluidity and curvature. Herein, we present the 2.8 Å resolution crystal structure of a thermally-stabilized human β(2)-adrenergic receptor bound to cholesterol and the partial in...

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Main Authors: Hanson, Michael A., Cherezov, Vadim, Roth, Christopher B., Griffith, Mark T., Jaakola, Veli-Pekka, Chien, Ellen Y. T., Velasquez, Jeffrey, Kuhn, Peter, Stevens, Raymond C.
Formato: Artigo
Idioma:Inglês
Publicado em: 2008
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Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2601552/
https://ncbi.nlm.nih.gov/pubmed/18547522
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2008.05.001
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