1yvl
From Proteopedia
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| , resolution 3.0Å | |||||||
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| Ligands: | , | ||||||
| Gene: | STAT1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Unphosphorylated STAT1
Contents |
Overview
The crystal structure has been determined at 3.0 A resolution for an unphosphorylated STAT1 (1-683) complexed with a phosphopeptide derived from the alpha chain of interferon gamma (IFNgamma) receptor. Two dimer interfaces are seen, one between the N domains (NDs) (amino acid residues 1-123) and the other between the core fragments (CFs) (residues 132-683). Analyses of the wild-type (wt) and mutant STAT1 proteins by static light scattering, analytical ultracentrifugation, and coimmunoprecipitation suggest that STAT1 is predominantly dimeric prior to activation, and the dimer is mediated by the ND interactions. The connecting region between the ND and the CF is flexible and allows two interconvertable orientations of the CFs, termed "antiparallel" or "parallel," as determined by SH2 domain orientations. Functional implications of these dimer conformations are discussed. Also revealed in this structure is the detailed interaction between STAT1 SH2 domain and its docking site on IFNgamma receptor.
Disease
Known disease associated with this structure: Mycobacterial infection, atypical, familial disseminated OMIM:[600555], STAT1 deficiency, complete OMIM:[600555]
About this Structure
1YVL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural bases of unphosphorylated STAT1 association and receptor binding., Mao X, Ren Z, Parker GN, Sondermann H, Pastorello MA, Wang W, McMurray JS, Demeler B, Darnell JE Jr, Chen X, Mol Cell. 2005 Mar 18;17(6):761-71. PMID:15780933
Page seeded by OCA on Mon Mar 31 01:24:13 2008
