A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor.

ABSTRACT:

Background

Bone morphogenetic proteins (BMPs) are key regulators in the embryonic development and postnatal tissue homeostasis in all animals. Loss of function or dysregulation of BMPs results in severe diseases or even lethality. Like transforming growth factors beta (TGF-betas), activins, growth and differentiation factors (GDFs) and other members of the TGF-beta superfamily, BMPs signal by assembling two types of serine/threonine-kinase receptor chains to form a hetero-oligomeric ligand-receptor complex. BMP ligand receptor interaction is highly promiscuous, i.e. BMPs bind more than one receptor of each subtype, and a receptor bind various ligands. The activin type II receptors are of particular interest, since they bind a large number of diverse ligands. In addition they act as

SUBMITTER: Weber D 

PROVIDER: S-EPMC1802081 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature