1b6c

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spinqualitylabelsall models 1b6c, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: Aortic aneurysm, familial thoracic 5 OMIM:[190181], Furlong syndrome OMIM:[190181], Loeys-Dietz syndrome OMIM:[190181]

About this Structure

1B6C is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.

Reference

Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12., Huse M, Chen YG, Massague J, Kuriyan J, Cell. 1999 Feb 5;96(3):425-36. PMID:10025408

Page seeded by OCA on Mon Nov 12 16:06:31 2007