2K3G: NMR structure analysis of a BMP receptor

The structure of the extracellular domain of BMP receptor IA was determined in solution by NMR spectroscopy and compared to its structure when bound to its ligand BMP-2. While most parts of the secondary structure are highly conserved between the bound and unbound forms, large conformational rearrangements can be observed in the beta4beta5 loop of BMPR-IA, which is in contact with BMP-2 and harbors the main binding determinants for the BMPR-IA-BMP-2 interaction. In its unbound form, helix alpha1 in BMPR-IA, which is in the center of the binding epitope for BMP-2, is missing. Since BMP-2 also shows conformational changes in the type I receptor epitope upon binding to BMPR-IA, both binding partners pass through an induced fit mechanism to adapt their binding interfaces to a given interaction surface. The inherent flexibility of both partners possibly explains the promiscuous ligand-receptor interaction observed in the BMP protein superfamily.
PDB ID: 2K3GDownload
MMDB ID: 68470
PDB Deposition Date: 2008/5/7
Updated in MMDB: 2008/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2K3G
Label Count Molecule
Protein (1 molecule)
Bone Morphogenetic Protein Receptor Type-1a(Gene symbol: BMPR1A)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB