Abstract:
:The molecular dynamics (MD) simulations study in the formation of the complex between compound SWR-0342SA and beta-ARs suggested that upon binding SWR-0342SA stimulates receptor activation through residues network (Asp104, Leu335 in beta(1)-AR; Asp117, Ser209, Leu303, Ser191 in beta(3)-AR) in an active conformation state. The models suggest that the structural origin of the selectivity of SWR-0342SA to beta(3)-AR vs. beta(1)-AR comes from the following results: (a) the tight interaction between the agonist and the TMs 3, 5, 6 and 2 nd EC loop. Asp117 interacts with the cationic amino group of the agonist molecule. (b) Additional contacts are done with Ser209, Leu303 and Ser191. These results are in good agreement with the binding affinities (pKi values) of SWR-0342SA to beta-AR family expressed in recombinant mammalian cells.
journal_name
Life Scijournal_title
Life sciencesauthors
Ahmed M,Ishiguro M,Nagatomo Tdoi
10.1016/j.lfs.2005.09.023subject
Has Abstractpub_date
2006-03-20 00:00:00pages
2019-23issue
17eissn
0024-3205issn
1879-0631pii
S0024-3205(05)01053-2journal_volume
78pub_type
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