Ontology highlight
ABSTRACT:
SUBMITTER: Walsh ST
PROVIDER: S-EPMC535364 | biostudies-literature | 2004 Dec
REPOSITORIES: biostudies-literature
Walsh Scott T R ST Sylvester Juliesta E JE Kossiakoff Anthony A AA
Proceedings of the National Academy of Sciences of the United States of America 20041124 49
Growth hormone regulates its biological properties via a sequential hormone-induced receptor homodimerization mechanism. Using a mutagenesis-scanning analysis of 81 single and 32 pairwise double mutations, we show that the hormone's two spatially distal receptor binding sites (Site1 and Site2) are allosterically coupled. These allosteric effects are focused among a relatively few residues centered around the interaction between Asp-116 of the hormone and Trp-169 of the receptor in Site2. A rearr ...[more]