Peptide self-aggregation and peptide complementarity as bases for the evolution of peptide receptors: a review.
This paper reviews the three major theories of peptide receptor evolution: (1) Dwyer's theory that peptide receptors evolved from self-aggregating peptides; (2) Root-Bernstein's theory that peptide receptors evolved from functionally and structurally complementary peptides; and (3) Blalock's theory that receptors evolved from hydropathically complementary sequences encoded in the antisense strand of the DNA encoding each peptide. The evidence to date suggests that the co-yevolution of peptides and their receptors is strongly constrained by one or more of these physicochemically based mechanisms, which argues against a random or frozen accident' model. The data also suggest that structure and function are integrally related from the earliest steps of receptor-ligand evolution so that peptide functionality is non-random and highly conserved in its origin. The result is a molecular paleontology' that reveals the evolutionary constraints that shaped the interaction of structure and function.
Root-Bernstein
Robert S
RS
Department of Physiology, 2174 Biomedical and Physical Sciences Building, Michigan State University, East Lansing, MI 48824 USA. rootbern@msu.edu
D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D006801:Humans; D008956:Models, Chemical; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010802:Phylogeny; D018000:Receptors, Peptide / Q000737:chemistry* / Q000145:classification / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D010455:Peptides; D018000:Receptors, Peptide