Dimerization of the lutropin receptor: insights from computational modeling.
A computational approach based upon rigid-body docking, ad hoc filtering, and cluster analysis has been carried out to predict likely interfaces in LHR homodimers. Quaternary structure predictions emphasize the role of helices 4, 5 and 6, with prominence to helix 4, in mediating inter-monomer interactions. Intermolecular interactions essentially involve the transmembrane domains rather than the hydrophilic loops and do not implicate disulfide bridges.Collectively, molecular dynamics simulations on the isolated receptor and computational modeling of LHR homodimerization suggest that mutation-induced LHR activation favors H4-H4 contacts involving the highly conserved W491 from both the receptors monomers.
Fanelli
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Department of Chemistry and Dulbecco Telethon Institute (DTI), University of Modena e Reggio Emilia, Via Campi 183, 41100 Modena, Italy. fanelli@unimo.it
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D019281:Dimerization; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011974:Receptors, LH / Q000737:chemistry* / Q000378:metabolism*; D012243:Rhodopsin / Q000737:chemistry; D013329:Structure-Activity Relationship
D011974:Receptors, LH; D012243:Rhodopsin