Evolution of minimal specificity and promiscuity in steroid hormone receptors.

ABSTRACT: Most proteins are regulated by physical interactions with other molecules; some are highly specific, but others interact with many partners. Despite much speculation, we know little about how and why specificity/promiscuity evolves in natural proteins. It is widely assumed that specific proteins evolved from more promiscuous ancient forms and that most proteins' specificity has been tuned to an optimal state by selection. Here we use ancestral protein reconstruction to trace the evolutionary history of ligand recognition in the steroid hormone receptors (SRs), a family of hormone-regulated animal transcription factors. We resurrected the deepest ancestral proteins in the SR family and characterized the structure-activity relationships by which they distinguished among ligands. We found tha

SUBMITTER: Eick GN 

PROVIDER: S-EPMC3499368 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature