3cwg | pdb_00003cwg

Unphosphorylated mouse STAT3 core fragment

spinqualitylabelsall models 3cwg, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cwg is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.05Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function STAT3_MOUSE Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. STAT3B interacts with the N-terminal part of JUN to activate such promoters in a cooperative way. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Signal transducers and activators of transcription (STATs) are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. Here we report a 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment. The overall monomeric structure is very similar to that of the phosphorylated STAT3 core fragment. However, the dimer interface observed in the unphosphorylated STAT1 core fragment structure is absent in the STAT3 structure. Solution studies further demonstrate that the core fragment of STAT3 is primarily monomeric. Mutations corresponding to those in STAT1, which lead to disruption of the core fragment interface and prolonged tyrosine phosphorylation, show little or no effect on the tyrosine phosphorylation kinetics of STAT3. These results highlight the structural and biochemical differences between STAT3 and STAT1, and suggest different regulation mechanisms of these two proteins. Crystal structure of unphosphorylated STAT3 core fragment.,Ren Z, Mao X, Mertens C, Krishnaraj R, Qin J, Mandal PK, Romanowski MJ, McMurray JS, Chen X Biochem Biophys Res Commun. 2008 Sep 12;374(1):1-5. Epub 2008 Apr 21. PMID:18433722 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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