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Peptide self‐aggregation and peptide complementarity as bases for the evolution of peptide receptors: a review
Author(s) -
RootBernstein Robert S.
Publication year - 2005
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.690
Subject(s) - peptide , receptor , complementarity (molecular biology) , function (biology) , biology , computational biology , evolutionary biology , biophysics , biochemistry , genetics
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. Copyright © 2004 John Wiley & Sons, Ltd.