1uus

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(New page: 200px<br /><applet load="1uus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uus, resolution 2.8&Aring;" /> '''STRUCTURE OF AN ACTIV...)
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caption="1uus, resolution 2.8&Aring;" />
caption="1uus, resolution 2.8&Aring;" />
'''STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM'''<br />
'''STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1UUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UUS OCA].
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1UUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUS OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Fukuzawa, M.]]
[[Category: Fukuzawa, M.]]
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[[Category: Muller, C.W.]]
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[[Category: Muller, C W.]]
[[Category: Petosa, C.]]
[[Category: Petosa, C.]]
[[Category: Ravelli, R.]]
[[Category: Ravelli, R.]]
[[Category: Soler-Lopez, M.]]
[[Category: Soler-Lopez, M.]]
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[[Category: Williams, J.G.]]
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[[Category: Williams, J G.]]
[[Category: dictyostelium]]
[[Category: dictyostelium]]
[[Category: sh2]]
[[Category: sh2]]
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[[Category: transducer]]
[[Category: transducer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:25:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:32 2008''

Revision as of 13:28, 21 February 2008


1uus, resolution 2.8Å

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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

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