3 research outputs found
Insights from the analysis of conserved motifs and permitted amino acid exchanges in the human, the fly and the worm GPCR clusters
G-protein coupled receptors (GPCRs) belong to biologically important and functionally diverse and largest super family of
membrane proteins. GPCRs retain a characteristic membrane topology of seven alpha helices with three intracellular, three
extracellular loops and flanking N' and C' terminal residues. Subtle differences do exist in the helix boundaries (TM-domain), loop
lengths, sequence features such as conserved motifs, and substituting amino acid patterns and their physiochemical properties
amongst these sequences (clusters) at intra-genomic and inter-genomic level (please re-phrase into 2 statements for clarity). In the
current study, we employ prediction of helix boundaries and scores derived from amino acid substitution exchange matrices to
identify the conserved amino acid residues (motifs) as consensus in aligned set of homologous GPCR sequences. Co-clustered
GPCRs from human and other genomes, organized as 32 clusters, were employed to study the amino acid conservation patterns
and species-specific or cluster-specific motifs. Critical analysis on sequence composition and properties provide clues to connect
functional relevance within and across genome for vast practical applications such as design of mutations and understanding of
disease-causing genetic abnormalities