Nanoscale structure of the BMP antagonist chordin supports cooperative BMP binding

• DOI: 10.1073/pnas.1404166111
• Publication Date: 2014-08-26T03:20:35Z
• Authors: Helen Troilo; Alexandra V. Zuk; Richard B. Tunnic...; Alexander P. Wohl; Richard Berry; Richard F. Collins; Thomas A. Jowitt; Gerhard Sengle; Clair Baldock
• Keywords: Chordin; Cleavage (geology); BMPR2

Significance Bone morphogenetic proteins (BMPs) are essential signaling molecules important in embryo development and maintaining tissue function adulthood. BMPs regulated outside the cell by inhibitors such as chordin. The structure of chordin is unknown extracellular generally not suitable for high-resolution methods. This study uses electron microscopy other techniques to determine shape human It has a compact horseshoe-shaped with terminal BMP-binding regions protruding prongs. spacing these domains supports cooperative binding arrangement BMPs. We compared BMP inhibition two truncated variants. Proteolytic cleavage little effect on BMP-4 BMP-7 but C-terminal makes better inhibitor.