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Ligand binding to the human MT2 melatonin receptor: The role of residues in transmembrane domains 3, 6, and 7
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SYSNO ASEP 0026822 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Ligand binding to the human MT2 melatonin receptor: The role of residues in transmembrane domains 3, 6, and 7 Title Vazba ligandu na lidský melatoninový receptor MT2 podtypu: role zbytků v transmembránových doménách 3, 6 a 7 Author(s) Mazna, Petr (FGU-C)
Berka, K. (CZ)
Jelínková, Irena (FGU-C)
Balík, Aleš (FGU-C) RID, ORCID
Svoboda, Petr (FGU-C) RID, ORCID
Obšilová, Veronika (FGU-C) RID, ORCID, SAI
Obšil, T. (CZ)
Teisinger, Jan (FGU-C) RIDSource Title Biochemical and Biophysical Research Communications. - : Elsevier - ISSN 0006-291X
Roč. 332, č. 3 (2005), s. 726-734Number of pages 9 s. Language eng - English Country US - United States Keywords MT2 melatonin receptor ; homology modeling ; binding study Subject RIV FR - Pharmacology ; Medidal Chemistry R&D Projects KJB5011308 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) GA309/02/1479 GA ČR - Czech Science Foundation (CSF) GA204/03/0714 GA ČR - Czech Science Foundation (CSF) GA309/04/0496 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z5011922 - FGU-C Annotation To further explore the mechanism of interaction between melatonin receptors and their ligands, our previously reported homology model of the ligand binding site of the hMT2 receptor was further refined and used to select residues within TM3, TM6 and TM7 potentially important for receptor-ligand interactions. These residues were mutated and binding properties of mutant receptors were characterized. In conclusion, our mutational analysis identified several new residues in in TM6 and TM7 that are essential for ligand binding to the hMT2 receptor Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2006
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