1uur: Difference between revisions

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[[Image:1uur.~~gif~~|left|200px]]

[[Image:1uur.png|left|200px]]

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

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

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_15053873}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15053873 is the PubMed ID number.

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==About this Structure==

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[[Category: Transcription factor]]

[[Category: Transducer]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 11~~:43:19 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:34:52 2008''

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-[[Image:1uur.gif|left|200px]]
+{{Seed}}
+[[Image:1uur.png|left|200px]]
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 {{STRUCTURE_1uur|  PDB=1uur  |  SCENE=  }}
-'''STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15053873}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15053873 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15053873}}
 ==About this Structure==
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 [[Category: Transcription factor]]
 [[Category: Transducer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:43:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:34:52 2008''