2fi2: Difference between revisions

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New page: left|200px<br /> <applet load="2fi2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fi2" /> '''Solution structure of the SCAN homodimer fr...
 
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[[Image:2fi2.gif|left|200px]]<br />
[[Image:2fi2.gif|left|200px]]<br /><applet load="2fi2" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2fi2" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2fi2" />
caption="2fi2" />
'''Solution structure of the SCAN homodimer from MZF-1/ZNF42'''<br />
'''Solution structure of the SCAN homodimer from MZF-1/ZNF42'''<br />


==Overview==
==Overview==
The SCAN domain mediates interactions between members of a subfamily of, zinc-finger transcription factors and is found in more than 60 C2H2 zinc, finger genes in the human genome, including the tumor suppressor gene, myeloid zinc finger 1 (MZF1). Glutathione-S-transferase pull-down assays, showed that the MZF1 SCAN domain self-associates, and a Kd value of 600 nM, was measured by intrinsic tryptophan fluorescence polarization. The MZF1, structure determined by NMR spectroscopy revealed a domain-swapped dimer., Each monomer consists of five alpha helices in two subdomains connected by, the alpha2-alpha3 loop. Residues from helix 3 of each monomer compose the, core of the dimer interface, while the alpha1-alpha2 loop and helix 2 pack, against helices 3 and 5 from the opposing monomer. Comprehensive sequence, analysis is coupled with the first high-resolution structure of a SCAN, dimer to provide an initial view of the recognition elements that govern, dimerization for this large family of transcription factors.
The SCAN domain mediates interactions between members of a subfamily of zinc-finger transcription factors and is found in more than 60 C2H2 zinc finger genes in the human genome, including the tumor suppressor gene myeloid zinc finger 1 (MZF1). Glutathione-S-transferase pull-down assays showed that the MZF1 SCAN domain self-associates, and a Kd value of 600 nM was measured by intrinsic tryptophan fluorescence polarization. The MZF1 structure determined by NMR spectroscopy revealed a domain-swapped dimer. Each monomer consists of five alpha helices in two subdomains connected by the alpha2-alpha3 loop. Residues from helix 3 of each monomer compose the core of the dimer interface, while the alpha1-alpha2 loop and helix 2 pack against helices 3 and 5 from the opposing monomer. Comprehensive sequence analysis is coupled with the first high-resolution structure of a SCAN dimer to provide an initial view of the recognition elements that govern dimerization for this large family of transcription factors.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2FI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FI2 OCA].  
2FI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FI2 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: CESG, Center.for.Eukaryotic.Structural.Genomics.]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
[[Category: Peterson, F.C.]]
[[Category: Peterson, F C.]]
[[Category: Sander, T.L.]]
[[Category: Sander, T L.]]
[[Category: Volkman, B.F.]]
[[Category: Volkman, B F.]]
[[Category: Waltner, J.K.]]
[[Category: Waltner, J K.]]
[[Category: center for eukaryotic structural genomics]]
[[Category: center for eukaryotic structural genomics]]
[[Category: cesg]]
[[Category: cesg]]
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[[Category: znf-42]]
[[Category: znf-42]]


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