1uus
From Proteopedia
|
STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM
Overview
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.
About this Structure
1UUS is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Nov 25 04:25:08 2007
