Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12 Journal Article
| Authors: | Huse, M.; Chen, Y. G.; Massagué, J.; Kuriyan, J. |
| Article Title: | Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12 |
| Abstract: | Activation of the type I TGFβ receptor (TβR-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 TβR- I, containing both the GS region and the catalytic domain, has been determined in complex with the FK506-binding protein FKBP12. TβR-I adopts an inactive conformation that is maintained by the unphosphorylated GS region. FKBP12 binds to the GS region of the receptor, capping the TβR-II phosphorylation sites and further stabilizing the inactive conformation of TβR-I. Certain structural features at the catalytic center of TβR-I are characteristic of tyrosine kinases rather than Ser/Thr kinases. |
| Keywords: | protein phosphorylation; nonhuman; protein conformation; protein protein interaction; enzyme activation; protein tyrosine kinase; amino acid sequence; molecular sequence data; protein-serine-threonine kinases; escherichia coli; peptide fragments; transforming growth factor beta receptor; receptors, transforming growth factor beta; cytoplasm; crystal structure; models, molecular; dimerization; crystallography, x-ray; protein structure, tertiary; protein-tyrosine kinases; protein structure, secondary; enzyme active site; fk 506 binding protein; activin receptors, type i; tacrolimus binding proteins; humans; priority journal; article; immunophilins |
| Journal Title: | Cell |
| Volume: | 96 |
| Issue: | 3 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1999-02-05 |
| Start Page: | 425 |
| End Page: | 436 |
| Language: | English |
| DOI: | 10.1016/s0092-8674(00)80555-3 |
| PUBMED: | 10025408 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
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