1miu: Difference between revisions

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 ==Structure of a BRCA2-DSS1 complex==
-<StructureSection load='1miu' size='340' side='right' caption='[[1miu]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='1miu' size='340' side='right'caption='[[1miu]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1miu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://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=1MIU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MIU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1miu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The April 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''RecA and Rad51''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_4 10.2210/rcsb_pdb/mom_2014_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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]] 3.1&#8491;</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=1miu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miu OCA], [http://pdbe.org/1miu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1miu RCSB], [http://www.ebi.ac.uk/pdbsum/1miu PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=1miu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miu OCA], [https://pdbe.org/1miu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1miu RCSB], [https://www.ebi.ac.uk/pdbsum/1miu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1miu ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/SEM1_HUMAN SEM1_HUMAN] Split hand-split foot malformation.
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/BRCA2_MOUSE BRCA2_MOUSE]] Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. In concert with NPM1, regulates centrosome duplication (By similarity).
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/1miu_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/1miu_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=1miu ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[BRCA 3D structures|BRCA 3D structures]]
-<div class="pdbe-citations 1miu" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Chen, P L]]
+[[Category: Mus musculus]]
-[[Category: Jeffrey, P D]]
+[[Category: RCSB PDB Molecule of the Month]]
-[[Category: Kinnucan, E]]
+[[Category: RecA and Rad51]]
-[[Category: Lee, W H]]
+[[Category: Chen PL]]
-[[Category: Miller, J]]
+[[Category: Jeffrey PD]]
-[[Category: Pavletich, N P]]
+[[Category: Kinnucan E]]
-[[Category: Sun, Y]]
+[[Category: Lee WH]]
-[[Category: Thoma, N H]]
+[[Category: Miller J]]
-[[Category: Yang, H]]
+[[Category: Pavletich NP]]
-[[Category: Zheng, N]]
+[[Category: Sun Y]]
-[[Category: Breast cancer susceptibility]]
+[[Category: Thoma NH]]
-[[Category: Dna-binding]]
+[[Category: Yang H]]
-[[Category: Gene regulation-antitumor protein complex]]
+[[Category: Zheng N]]
-[[Category: Tumor suppressor]]