Proteochemometric Modeling of Chimeric MC Receptors Interacting with MSH Peptides

Proteochemometric Modeling of Chimeric MC Receptors Interacting with MSH Peptides 

A method for assessing the interactions responsible for peptide selectivity was also developed, by creating a separate model in which the interaction activity was expressed as the MCjR selectivity of each peptide, rather than as absolute values for ligand-binding activity. Also here, a very good model was obtained (R2 = 0.92, Q2 = 0.72), which interestingly revealed that the MCjR selectivity of the peptides were primarily determined by interaction of their N termini with TM2/3 of the MCRs [12a], 

Proteochemometric Modeling of a, Adrenoceptors Using z Scale Descriptors for Amino Acids 

The above studies were conducted on chimeric receptors put together from the sequences of two receptors. Subsequent studies were directed at biopolymer sets containing larger variations. One of these studies utilized a set of chimeric and point-mutated oq-adrenoceptors (a,-Alls) that allowed a much richer description compared to the binary descriptions used above. The biopolymer set in the study comprised in total 18 a,-Alls, namely the wild-type ala, alb, and ald-ARs and 15 mutated oq-ARs. The latter had been constructed by exchanging TM segments of ala-AR with the corresponding segments of the alb or ald-ARs (i.e., cassette 

An even more detailed picture was obtained by analyzing the model that included both the cassette- and point-mutated receptors. For example, this model showed that the properties of the amino acid at sequence position 86 in TM region two of the otj-ARs are important for activity. Moreover, this model showed that the single amino acid at position 185 was responsible for almost all of the ZSOP values, although in the model based only on cassette-mutated receptors high ZSOP values were assigned to the whole TM region five. These results show that inclusion of 

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