A host-guest relationship in bone morphogenetic protein receptor-II defines specificity in ligand-receptor recognition.

ABSTRACT: One of the most intriguing questions confronting the bone morphogenetic protein family is the mechanism of ligand recognition, because there are more ligands than receptors. Crystal structures of two type II receptors, ActR-II and BMPR-II, are essentially identical, and a loop structure (A-loop) has been suggested to play a role in determining ligand specificity. A solution biophysical study showed mutations of several A-loop residues in these two receptors exert different ligand binding effects. Thus, the issues of mechanism of ligand recognition and specificity remain unresolved. We examined effects of mutations of residues Y40, G47, and S107 in BMPR-II. These residues are not identified as being in contact with the ligand in the BMP-7-BMPR-II complex but are found mutated in genetic dis

SUBMITTER: Yeh LC 

PROVIDER: S-EPMC3481545 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature