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Crystal structure of β-adrenergic receptor as a new template in homology modeling of GPCR. Application to serotonin 5-HT1A and 5-HT7 receptors |
Elżbieta Pieniążek 1, Mateusz Nowak 1, Andrzej J. Bojarski 1, Małgorzata Jarończyk 2, Zdzisław Chilmonczyk 2 |
1. Polish Academy of Sciences. Institute of Pharmacology, Smętna 12, Kraków 31-343, Poland |
Abstract |
When dificulties in receiving crystal structures appear, homology modeling aproach is the best way to obtain three dimensional structure of a protein. Procedure is realtively simple, but results depend on degree of similarity between a target and a template sequence. Since 2000 there was one available crystal structure of transmembrane domain of GPCR protein: the bovine rhodopsin. We, and others have previously shown that regardless of relatively low sequence identity, it was possible to obtain useful rhodopsin based models of serotonin receptors, such as 5-HT1A and 5HT7. In October 2007, a high resolution structure of another GPCR, beta-2 adrenergic receptor, was solved. Very close evolutionary relationships between 5-HT receptors and beta adrenoreceptors give us possibility to improve comparative models of serotonin receptors and to verify our previous results. New homology models will be used in a process of drug design and virtual screening. Acknowledgement |
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Presentation: Poster at VI Multidyscyplinarna Konferencja Nauki o Leku, by Elżbieta PieniążekSee On-line Journal of VI Multidyscyplinarna Konferencja Nauki o Leku Submitted: 2008-03-14 16:37 Revised: 2009-06-07 00:48 |