This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2fi2

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Solution structure of the SCAN homodimer from MZF-1/ZNF42

Structural highlights

2fi2 is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

MZF1_HUMAN Binds to target promoter DNA and functions as trancription regulator. Regulates transcription from the PADI1 and CDH2 promoter. May be one regulator of transcriptional events during hemopoietic development.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Le Mee S, Fromigue O, Marie PJ. Sp1/Sp3 and the myeloid zinc finger gene MZF1 regulate the human N-cadherin promoter in osteoblasts. Exp Cell Res. 2005 Jan 1;302(1):129-42. PMID:15541732 doi:http://dx.doi.org/10.1016/j.yexcr.2004.08.028
↑ Dong S, Ying S, Kojima T, Shiraiwa M, Kawada A, Mechin MC, Adoue V, Chavanas S, Serre G, Simon M, Takahara H. Crucial roles of MZF1 and Sp1 in the transcriptional regulation of the peptidylarginine deiminase type I gene (PADI1) in human keratinocytes. J Invest Dermatol. 2008 Mar;128(3):549-57. Epub 2007 Sep 13. PMID:17851584 doi:http://dx.doi.org/10.1038/sj.jid.5701048
↑ Peterson FC, Hayes PL, Waltner JK, Heisner AK, Jensen DR, Sander TL, Volkman BF. Structure of the SCAN domain from the tumor suppressor protein MZF1. J Mol Biol. 2006 Oct 13;363(1):137-47. Epub 2006 Jul 31. PMID:16950398 doi:10.1016/j.jmb.2006.07.063

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fi2"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2fi2.png|left|200px]]
-<!--
+==Solution structure of the SCAN homodimer from MZF-1/ZNF42==
-The line below this paragraph, containing "STRUCTURE_2fi2", creates the "Structure Box" on the page.
+<StructureSection load='2fi2' size='340' side='right'caption='[[2fi2]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2fi2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FI2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fi2 OCA], [https://pdbe.org/2fi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fi2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fi2 ProSAT], [https://www.topsan.org/Proteins/CESG/2fi2 TOPSAN]</span></td></tr>
-{{STRUCTURE_2fi2|  PDB=2fi2  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MZF1_HUMAN MZF1_HUMAN] Binds to target promoter DNA and functions as trancription regulator. Regulates transcription from the PADI1 and CDH2 promoter. May be one regulator of transcriptional events during hemopoietic development.<ref>PMID:15541732</ref> <ref>PMID:17851584</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/2fi2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fi2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Solution structure of the SCAN homodimer from MZF-1/ZNF42===
+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<ref>PMID:16950398</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16950398}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2fi2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16950398 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16950398}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FI2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FI2 OCA].
-==Reference==
-<ref group="xtra">PMID:16950398</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
+[[Category: Large Structures]]
-[[Category: Peterson, F C.]]
+[[Category: Peterson FC]]
-[[Category: Sander, T L.]]
+[[Category: Sander TL]]
-[[Category: Volkman, B F.]]
+[[Category: Volkman BF]]
-[[Category: Waltner, J K.]]
+[[Category: Waltner JK]]
-[[Category: Center for eukaryotic structural genomic]]
-[[Category: Cesg]]
-[[Category: Homodimer]]
-[[Category: Mzf-1]]
-[[Category: Protein structure initiative]]
-[[Category: Psi]]
-[[Category: Scan domain]]
-[[Category: Structural genomic]]
-[[Category: Transcription factor]]
-[[Category: Znf-42]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:42:38 2009''

2fi2

From Proteopedia

Current revision

Solution structure of the SCAN homodimer from MZF-1/ZNF42

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox