TI  - Crystal structure of the  <prot>BMP-2</prot> - <prot>BRIA</prot>  ectodomain complex.
PG  - 492-6
AB  - Bone morphogenetic proteins (BMPs) belong to the large <prot>transforming growth
      factor-beta</prot> (<prot>TGF-beta</prot>) superfamily of multifunctional cytokines. <prot>BMP-2</prot> can
      induce ectopic bone and cartilage formation in adult vertebrates and is
      involved in central steps in early embryonal development in animals.
      Signaling by these cytokines requires binding of two types of
      transmembrane serine/threonine receptor kinase chains classified as type I
      and type II. Here we report the crystal structure of  human dimeric <prot>BMP-2</prot> 
      in complex with two high affinity <prot><prot>BMP receptor IA</prot> extracellular domain</prot>
      (<prot>BRIAec</prot>) . The receptor chains bind to the 'wrist' epitopes of the   <prot>BMP-2 </prot> 
      dimer and contact both <prot>BMP-2</prot> monomers. No contacts exist between the
      receptor domains. The model reveals the structural basis for
      discrimination between type I and type II receptors and the variability of
      receptor-ligand interactions that is seen in BMP-<prot>TGF-beta</prot> systems.
AD  - Physiologische Chemie II, Biozentrum der Universitat Wurzburg, Germany.
