1ias
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(New page: 200px<br /> <applet load="1ias" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ias, resolution 2.9Å" /> '''CYTOPLASMIC DOMAIN O...)
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Revision as of 15:21, 12 November 2007
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CYTOPLASMIC DOMAIN OF UNPHOSPHORYLATED TYPE I TGF-BETA RECEPTOR CRYSTALLIZED WITHOUT FKBP12
Contents |
Overview
The type I TGF beta receptor (T beta R-I) is activated by phosphorylation, of the GS region, a conserved juxtamembrane segment located just, N-terminal to the kinase domain. We have studied the molecular mechanism, of receptor activation using a homogeneously tetraphosphorylated form of T, beta R-I, prepared using protein semisynthesis. Phosphorylation of the GS, region dramatically enhances the specificity of T beta R-I for the, critical C-terminal serines of Smad2. In addition, tetraphosphorylated T, beta R-I is bound specifically by Smad2 in a phosphorylation-dependent, manner and is no longer recognized by the inhibitory protein FKBP12. Thus, phosphorylation activates T beta R-I by switching the GS region from a, binding site for an inhibitor into a binding surface for substrate. Our, observations suggest that phosphoserine/phosphothreonine-dependent, localization is a key feature of the T beta R-I/Smad activation process.
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
1IAS is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
The TGF beta receptor activation process: an inhibitor- to substrate-binding switch., Huse M, Muir TW, Xu L, Chen YG, Kuriyan J, Massague J, Mol Cell. 2001 Sep;8(3):671-82. PMID:11583628
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