2mh2
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mh2]] 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=2MH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MH2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2mh2]] 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=2MH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MH2 FirstGlance]. <br> | ||
| - | </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=2mh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mh2 OCA], [https://pdbe.org/2mh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mh2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mh2 ProSAT]</span></td></tr> | + | </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=2mh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mh2 OCA], [https://pdbe.org/2mh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mh2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mh2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HOP2_MOUSE HOP2_MOUSE] Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3.<ref>PMID:9345291</ref> <ref>PMID:15192114</ref> <ref>PMID:16675459</ref> <ref>PMID:17639080</ref> <ref>PMID:17639081</ref> <ref>PMID:17426123</ref> | [https://www.uniprot.org/uniprot/HOP2_MOUSE HOP2_MOUSE] Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3.<ref>PMID:9345291</ref> <ref>PMID:15192114</ref> <ref>PMID:16675459</ref> <ref>PMID:17639080</ref> <ref>PMID:17639081</ref> <ref>PMID:17426123</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | The HOP2 protein is required for efficient double-strand break repair which ensures the proper synapsis of homologous chromosomes and normal meiotic progression. We previously showed that in vitro HOP2 shows two distinctive activities: when it is incorporated into a HOP2-MND1 heterodimer, it stimulates DMC1 and RAD51 recombination activities, and the purified HOP2 alone is proficient in promoting strand invasion. The structural and biochemical basis of HOP2 action in recombination are poorly understood; therefore, they are the focus of this work. Herein, we present the solution structure of the amino-terminal portion of mouse HOP2, which contains a typical winged helix DNA-binding domain. Together with NMR spectral changes in the presence of double-stranded DNA, protein docking on DNA, and mutation analysis to identify the amino acids involved in DNA coordination, our results on the three-dimensional structure of HOP2 provide key information on the fundamental structural and biochemical requirements directing the interaction of HOP2 with DNA. These results, in combination with mutational experiments showing the role of a coiled-coil structural feature involved in HOP2 self-association, allow us to explain important aspects of the function of HOP2 in recombination. | ||
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| - | Solution Structure and DNA-binding Properties of the Winged Helix Domain of the Meiotic Recombination HOP2 Protein.,Moktan H, Guiraldelli MF, Eyster CA, Zhao W, Lee CY, Mather T, Camerini-Otero RD, Sung P, Zhou DH, Pezza RJ J Biol Chem. 2014 May 23;289(21):14682-91. doi: 10.1074/jbc.M114.548180. Epub, 2014 Apr 6. PMID:24711446<ref>PMID:24711446</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2mh2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structural insights into the DNA recognition and protein interaction domains reveal fundamental homologous DNA pairing properties of HOP2
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Categories: Large Structures | Mus musculus | Camerini-Otero RD | Eyter CA | Guiraldelli MF | Moktan H | Pezza RJ | Sung P | Zhao W | Zhou DH
