3abe: Difference between revisions

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<StructureSection load='3abe' size='340' side='right'caption='[[3abe]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3abe' size='340' side='right'caption='[[3abe]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3abe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ABE FirstGlance]. <br>
<table><tr><td colspan='2'>[[3abe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ABE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3abd|3abd]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">REV7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), REV3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3abe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abe OCA], [https://pdbe.org/3abe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3abe RCSB], [https://www.ebi.ac.uk/pdbsum/3abe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3abe ProSAT]</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=3abe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abe OCA], [https://pdbe.org/3abe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3abe RCSB], [https://www.ebi.ac.uk/pdbsum/3abe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3abe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref> [[https://www.uniprot.org/uniprot/DPOLZ_HUMAN DPOLZ_HUMAN]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.
[https://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/3abe_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/3abe_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 3abe" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3abe" style="background-color:#fffaf0;"></div>
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Akashi, S]]
[[Category: Akashi S]]
[[Category: Hara, K]]
[[Category: Hara K]]
[[Category: Hashimoto, H]]
[[Category: Hashimoto H]]
[[Category: Kobayashi, S]]
[[Category: Kobayashi S]]
[[Category: Kogame, T]]
[[Category: Kogame T]]
[[Category: Murakumo, Y]]
[[Category: Murakumo Y]]
[[Category: Sato, M]]
[[Category: Sato M]]
[[Category: Shimizu, T]]
[[Category: Shimizu T]]
[[Category: Takeda, S]]
[[Category: Takeda S]]
[[Category: Unzai, S]]
[[Category: Unzai S]]
[[Category: Cell cycle]]
[[Category: Cell cycle-replication complex]]
[[Category: Cell division]]
[[Category: Dna damage]]
[[Category: Dna polymerase]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Dna-binding]]
[[Category: Dna-directed dna polymerase]]
[[Category: Horma]]
[[Category: Mitosis]]
[[Category: Translesion synthesis]]

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