1uus
From Proteopedia
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| - | [[Image:1uus.jpg|left|200px]] | + | [[Image:1uus.jpg|left|200px]] |
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| - | '''STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM''' | + | {{Structure |
| + | |PDB= 1uus |SIZE=350|CAPTION= <scene name='initialview01'>1uus</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS DNA-UNBOUND FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UUS is a [ | + | 1UUS is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15053873 15053873] |
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:07 2008'' |
Revision as of 12:37, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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