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1uur

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(New page: 200px<br /><applet load="1uur" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uur, resolution 2.7&Aring;" /> '''STRUCTURE OF AN ACTIV...)
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Revision as of 02:17, 25 November 2007

Image:1uur.gif

1uur, resolution 2.7Å

Drag the structure with the mouse to rotate

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

1UUR 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

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