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Cell. 1999 Feb 5;96(3):425-36.

Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12.

Author information

1
Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021, USA.

Abstract

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.

PMID:
10025408
DOI:
10.1016/s0092-8674(00)80555-3
[Indexed for MEDLINE]
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