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1: Cell. 1999 Feb 5;96(3):425-36.Click here to read Links

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

Huse M, Chen YG, Massagué J, Kuriyan J.

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

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 [PubMed - indexed for MEDLINE]

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