2kvh: Difference between revisions

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 ==Structure of the three-Cys2His2 domain of mouse testis zinc finger protein==
-<StructureSection load='2kvh' size='340' side='right' caption='[[2kvh]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='2kvh' size='340' side='right'caption='[[2kvh]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kvh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KVH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KVH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kvf|2kvf]], [[2kvg|2kvg]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kvh OCA], [http://pdbe.org/2kvh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kvh RCSB], [http://www.ebi.ac.uk/pdbsum/2kvh PDBsum]</span></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=2kvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kvh OCA], [https://pdbe.org/2kvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kvh RCSB], [https://www.ebi.ac.uk/pdbsum/2kvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kvh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ZBT32_MOUSE ZBT32_MOUSE]] DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor (By similarity). Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells.<ref>PMID:11279021</ref>
+[https://www.uniprot.org/uniprot/ZBT32_MOUSE ZBT32_MOUSE] DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor (By similarity). Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells.<ref>PMID:11279021</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The C-terminal three-Cys(2)His(2) zinc-finger domain (TZD) of mouse testis zinc-finger protein binds to the 5'-TGTACAGTGT-3' at the Aie1 (aurora-C) promoter with high specificity. Interestingly, the primary sequence of TZD is unique, possessing two distinct linkers, TGEKP and GAAP, and distinct residues at presumed DNA binding sites at each finger, especially finger 3. A K(d) value of approximately 10(-8) M was obtained from surface plasmon resonance analysis for the TZD-DNA complex. NMR structure of the free TZD showed that each zinc finger forms a typical beta beta alpha fold. On binding to DNA, chemical shift perturbations and the R(2) transverse relaxation rate in finger 3 are significantly smaller than those in fingers 1 and 2, which indicates that the DNA binding affinity in finger 3 is weaker. Furthermore, the shift perturbations between TZD in complex with the cognate DNA and its serial mutants revealed that both ADE7 and CYT8, underlined in 5'-ATATGTACAGTGTTAT-3', are critical in specific binding, and the DNA binding in finger 3 is sequence independent. Remarkably, the shift perturbations in finger 3 on the linker mutation of TZD (GAAP mutated to TGEKP) were barely detected, which further indicates that finger 3 does not play a critical role in DNA sequence-specific recognition. The complex model showed that residues important for DNA binding are mainly located on positions -1, 2, 3, and 6 of alpha-helices in fingers 1 and 2. The DNA sequence and nonsequence-specific bindings occurring simultaneously in TZD provide valuable information for better understanding of protein-DNA recognition.
+Structure and DNA binding characteristics of the three-Cys(2)His(2) domain of mouse testis zinc finger protein.,Chou CC, Lou YC, Tang TK, Chen C Proteins. 2010 Aug 1;78(10):2202-12. doi: 10.1002/prot.22732. PMID:20544958<ref>PMID:20544958</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2kvh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Chen, C]]
+[[Category: Mus musculus]]
-[[Category: Chou, C C]]
+[[Category: Chen C]]
-[[Category: Lou, Y C]]
+[[Category: Chou C-C]]
-[[Category: Metal-binding]]
+[[Category: Lou Y-C]]
-[[Category: Protein/dna]]
-[[Category: Transcription]]
-[[Category: Zinc-finger]]