1YVL

Structure of Unphosphorylated STAT1

Summary for 1YVL

• Entry DOI: 10.2210/pdb1yvl/pdb
• Descriptor: Signal transducer and activator of transcription 1-alpha/beta, 5-residue peptide, GOLD ION (3 entities in total)
• Functional Keywords: signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P42224
• Total number of polymer chains: 4
• Total formula weight: 161963.84

Authors

Mao, X.,Ren, Z.,Parker, G.N.,Sondermann, H.,Pastorello, M.A.,Wang, W.,McMurray, J.S.,Demeler, B.,Darnell Jr., J.E.,Chen, X. (deposition date: 2005-02-16, release date: 2005-03-22, Last modification date: 2024-10-30)

Primary citation

Mao, X.,Ren, Z.,Parker, G.N.,Sondermann, H.,Pastorello, M.A.,Wang, W.,McMurray, J.S.,Demeler, B.,Darnell, J.E.,Chen, X.
Structural bases of unphosphorylated STAT1 association and receptor binding.
Mol.Cell, 17:761-771, 2005

PubMed Abstract: 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.

PubMed: 15780933
DOI: 10.1016/j.molcel.2005.02.021

Experimental method

X-RAY DIFFRACTION (3 Å)