2fi2
From Proteopedia
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|GENE= ZNF42, MZF1, ZSCAN6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ZNF42, MZF1, ZSCAN6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00431 LER]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00431 LER]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fi2 OCA], [http://www.ebi.ac.uk/pdbsum/2fi2 PDBsum | + | |RELATEDENTRY= |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fi2 OCA], [http://www.ebi.ac.uk/pdbsum/2fi2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fi2 RCSB]</span> | ||
}} | }} | ||
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==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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Mental retardation syndrome, X-linked, Siderius type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300560 300560]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: znf-42]] | [[Category: znf-42]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:03:05 2008'' |
Revision as of 00:03, 31 March 2008
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| Gene: | ZNF42, MZF1, ZSCAN6 (Homo sapiens) | ||||||
| Domains: | LER | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the SCAN homodimer from MZF-1/ZNF42
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.
About this Structure
2FI2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the SCAN domain from the tumor suppressor protein MZF1., Peterson FC, Hayes PL, Waltner JK, Heisner AK, Jensen DR, Sander TL, Volkman BF, J Mol Biol. 2006 Oct 13;363(1):137-47. Epub 2006 Jul 31. PMID:16950398
Page seeded by OCA on Mon Mar 31 03:03:05 2008
Categories: Homo sapiens | Single protein | CESG, Center for Eukaryotic Structural Genomics. | Peterson, F C. | Sander, T L. | Volkman, B F. | Waltner, J K. | Center for eukaryotic structural genomic | Cesg | Homodimer | Mzf-1 | Protein structure initiative | Psi | Scan domain | Structural genomic | Transcription factor | Znf-42
