PMC:4504005 / 27268-28310 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4504005","sourcedb":"PMC","sourceid":"4504005","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4504005","text":"Mapping the receptor mutagenesis data (Figures 4 and 5) onto the surface of the receptor structures (Figures 7A and 7B) suggests that CGRP binds in a similar manner to CGRPmut and that the structures are good models for full-length CGRP and AM binding to intact receptors. Mutation of CLR residues that form the shared binding site diminished CGRP and AM potencies, and the effects of some of the mutations were similar for both peptides (e.g., F92). Noteworthy divergent effects of several mutations support the differences in the structures. CLR D94 was far more important for CGRP action than AM, consistent with the crucial role of D94 in contacting CGRP T30 and its less important role in contacting the AM main chain. CLR R119A diminished the potency of CGRP much more than that of AM, which may reflect an important role for the different R119 conformations observed in the two structures. CLR W72A was more deleterious for AM action than CGRP, which is consistent with the greater number of AM contacts to CLR W72 as compared to CGRP.","tracks":[]}