Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12.
Activation of the type I TGFbeta receptor (TbetaR-I) requires phosphorylation of a regulatory segment known as the GS region, located upstream of the serine/threonine kinase domain in the cytoplasmic portion of the receptor. The crystal structure of a fragment of unphosphorylated TbetaR-I, containing both the GS region and the catalytic domain, has been determined in complex with the FK506-binding protein FKBP12. TbetaR-I adopts an inactive conformation that is maintained by the unphosphorylated GS region. FKBP12 binds to the GS region of the receptor, capping the TbetaR-II phosphorylation sites and further stabilizing the inactive conformation of TbetaR-I. Certain structural features at the catalytic center of TbetaR-I are characteristic of tyrosine kinases rather than Ser/Thr kinases.[1]References
- Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Huse, M., Chen, Y.G., Massagué, J., Kuriyan, J. Cell (1999) [Pubmed]
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