1uur | pdb_00001uur

STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM

spinqualitylabelsall models 1uur, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uur is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: PTR Related: 1uus Resources: FirstGlance, OCA, RCSB, PDBsum 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 Dd-STATa is a STAT protein which transcriptionally regulates cellular differentiation in Dictyostelium discoideum, the only non-metazoan known to employ SH2 domain signaling. The 2.7 A crystal structure of a tyrosine phosphorylated Dd-STATa homodimer reveals a four-domain architecture similar to that of mammalian STATs 1 and 3, but with an inverted orientation for the coiled-coil domain. Dimerization is mediated by SH2 domain:phosphopeptide interactions and by a direct interaction between SH2 domains. The unliganded Dd-STATa dimer adopts a fully extended conformation remarkably different from that of the DNA-bound mammalian STATs, implying a large conformational change upon target site recognition. Buried hydrophilic residues predicted to destabilize the coiled-coil domain suggest how hydrophobic residues may become exposed and mediate nuclear export. Functional and evolutionary implications for metazoan STAT proteins are discussed. Structure of an activated Dictyostelium STAT in its DNA-unbound form.,Soler-Lopez M, Petosa C, Fukuzawa M, Ravelli R, Williams JG, Muller CW Mol Cell. 2004 Mar 26;13(6):791-804. PMID:15053873 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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