1mje

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Current revision (07:44, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1mje' size='340' side='right'caption='[[1mje]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='1mje' size='340' side='right'caption='[[1mje]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1mje]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1mje]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJE FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iyj|1iyj]]</div></td></tr>
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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]] 3.5&#8491;</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=1mje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mje OCA], [https://pdbe.org/1mje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mje RCSB], [https://www.ebi.ac.uk/pdbsum/1mje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mje 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=1mje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mje OCA], [https://pdbe.org/1mje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mje RCSB], [https://www.ebi.ac.uk/pdbsum/1mje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mje ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SEM1_HUMAN SEM1_HUMAN] Split hand-split foot malformation.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DSS1_HUMAN DSS1_HUMAN]] Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis.<ref>PMID:15117943</ref>
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[https://www.uniprot.org/uniprot/SEM1_HUMAN SEM1_HUMAN] Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:15117943). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and thus transcription-associated genomic instability. R-loop accumulation increases in SEM1-depleted cells.<ref>PMID:1317798</ref> <ref>PMID:15117943</ref> <ref>PMID:22307388</ref> <ref>PMID:24896180</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1mje ConSurf].
</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=1mje ConSurf].
<div style="clear:both"></div>
<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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Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers.
 
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BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure.,Yang H, Jeffrey PD, Miller J, Kinnucan E, Sun Y, Thoma NH, Zheng N, Chen PL, Lee WH, Pavletich NP Science. 2002 Sep 13;297(5588):1837-48. PMID:12228710<ref>PMID:12228710</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 1mje" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Chen, P L]]
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[[Category: Chen PL]]
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[[Category: Jeffrey, P D]]
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[[Category: Jeffrey PD]]
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[[Category: Kinnucan, E]]
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[[Category: Kinnucan E]]
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[[Category: Lee, W H]]
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[[Category: Lee WH]]
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[[Category: Miller, J]]
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[[Category: Miller J]]
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[[Category: Pavletich, N P]]
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[[Category: Pavletich NP]]
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[[Category: Sun, Y]]
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[[Category: Sun Y]]
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[[Category: Thoma, N H]]
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[[Category: Thoma NH]]
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[[Category: Yang, H]]
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[[Category: Yang H]]
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[[Category: Zheng, N]]
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[[Category: Zheng N]]
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[[Category: Breast cancer susceptibility]]
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[[Category: Dna-binding]]
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[[Category: Gene regulation-antitumor protein-dna complex]]
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[[Category: Tumor suppressor]]
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Current revision

STRUCTURE OF A BRCA2-DSS1-SSDNA COMPLEX

PDB ID 1mje

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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