3abe

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{{Seed}}
 
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[[Image:3abe.png|left|200px]]
 
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==Structure of human REV7 in complex with a human REV3 fragment in a tetragonal crystal==
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The line below this paragraph, containing "STRUCTURE_3abe", creates the "Structure Box" on the page.
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<StructureSection load='3abe' size='340' side='right'caption='[[3abe]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_3abe| PDB=3abe | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/3abe_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3abe ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DNA polymerase zeta (Polzeta) is an error-prone DNA polymerase involved in translesion DNA synthesis. Polzeta consists of two subunits: the catalytic REV3, which belongs to B family DNA polymerase, and the noncatalytic REV7. REV7 also interacts with REV1 polymerase, which is an error-prone Y family DNA polymerase and is also involved in translesion DNA synthesis. Cells deficient in one of the three REV proteins and those deficient in all three proteins show similar phenotype, indicating the functional collaboration of the three REV proteins. REV7 interacts with both REV3 and REV1 polymerases, but the structure of REV7 or REV3, as well as the structural and functional basis of the REV1-REV7 and REV3-REV7 interactions, remains unknown. Here we show the first crystal structure of human REV7 in complex with a fragment of human REV3 polymerase (residues 1847-1898) and reveal the mechanism underlying REV7-REV3 interaction. The structure indicates that the interaction between REV7 and REV3 creates a structural interface for REV1 binding. Furthermore, we show that the REV7-mediated interactions are responsible for DNA damage tolerance. Our results highlight the function of REV7 as an adapter protein to recruit Polzeta to a lesion site. REV7 is alternatively called MAD2B or MAD2L2 and also involved in various cellular functions such as signal transduction and cell cycle regulation. Our results will provide a general structural basis for understanding the REV7 interaction.
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===Structure of human REV7 in complex with a human REV3 fragment in a tetragonal crystal===
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Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1.,Hara K, Hashimoto H, Murakumo Y, Kobayashi S, Kogame T, Unzai S, Akashi S, Takeda S, Shimizu T, Sato M J Biol Chem. 2010 Apr 16;285(16):12299-307. Epub 2010 Feb 17. PMID:20164194<ref>PMID:20164194</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3abe" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20164194}}, adds the Publication Abstract to the page
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20164194 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20164194}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3ABE is a 2 chains structure with sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:20164194</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Akashi, S.]]
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[[Category: Large Structures]]
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[[Category: Hara, K.]]
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[[Category: Akashi S]]
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[[Category: Hashimoto, H.]]
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[[Category: Hara K]]
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[[Category: Kobayashi, S.]]
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[[Category: Hashimoto H]]
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[[Category: Kogame, T.]]
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[[Category: Kobayashi S]]
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[[Category: Murakumo, Y.]]
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[[Category: Kogame T]]
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[[Category: Sato, M.]]
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[[Category: Murakumo Y]]
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[[Category: Shimizu, T.]]
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[[Category: Sato M]]
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[[Category: Takeda, S.]]
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[[Category: Shimizu T]]
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[[Category: Unzai, S.]]
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[[Category: Takeda S]]
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[[Category: Cell cycle]]
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[[Category: Unzai S]]
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[[Category: Cell cycle-replication complex]]
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[[Category: Cell division]]
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[[Category: Dna damage]]
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[[Category: Dna polymerase]]
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[[Category: Dna repair]]
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[[Category: Dna replication]]
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[[Category: Dna-binding]]
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[[Category: Dna-directed dna polymerase]]
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[[Category: Horma]]
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[[Category: Mitosis]]
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[[Category: Polymorphism]]
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[[Category: Translesion synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 08:25:30 2010''
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Current revision

Structure of human REV7 in complex with a human REV3 fragment in a tetragonal crystal

PDB ID 3abe

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