A selection fit mechanism in BMP receptor IA as a possible source for BMP ligand-receptor promiscuity.

ABSTRACT:

Background

Members of the TGF-β superfamily are characterized by a highly promiscuous ligand-receptor interaction as is readily apparent from the numeral discrepancy of only seven type I and five type II receptors available for more than 40 ligands. Structural and functional studies have been used to address the question of how specific signals can be deduced from a limited number of receptor combinations and to unravel the molecular mechanisms underlying the protein-protein recognition that allow such limited specificity.

Principal findings

In this study we have investigated how an antigen binding antibody fragment (Fab) raised against the extracellular domain of the BMP receptor type IA (BMPR-IA) recognizes the receptor's BMP-2 binding epitope and thereby neutralizes BMP-2

SUBMITTER: Harth S 

PROVIDER: S-EPMC2946932 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature