1miu
From Proteopedia
(Difference between revisions)
m (Protected "1miu" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[ | + | ==Structure of a BRCA2-DSS1 complex== |
| + | <StructureSection load='1miu' size='340' side='right' caption='[[1miu]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1miu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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> | ||
| + | </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> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=1miu RCSB], [http://www.ebi.ac.uk/pdbsum/1miu PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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). | ||
| + | == 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> | ||
| + | <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]. | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Chen, P L | + | [[Category: Chen, P L]] |
| - | [[Category: Jeffrey, P D | + | [[Category: Jeffrey, P D]] |
| - | [[Category: Kinnucan, E | + | [[Category: Kinnucan, E]] |
| - | [[Category: Lee, W H | + | [[Category: Lee, W H]] |
| - | [[Category: Miller, J | + | [[Category: Miller, J]] |
| - | [[Category: Pavletich, N P | + | [[Category: Pavletich, N P]] |
| - | [[Category: Sun, Y | + | [[Category: Sun, Y]] |
| - | [[Category: Thoma, N H | + | [[Category: Thoma, N H]] |
| - | [[Category: Yang, H | + | [[Category: Yang, H]] |
| - | [[Category: Zheng, N | + | [[Category: Zheng, N]] |
[[Category: Breast cancer susceptibility]] | [[Category: Breast cancer susceptibility]] | ||
[[Category: Dna-binding]] | [[Category: Dna-binding]] | ||
[[Category: Gene regulation-antitumor protein complex]] | [[Category: Gene regulation-antitumor protein complex]] | ||
[[Category: Tumor suppressor]] | [[Category: Tumor suppressor]] | ||
Revision as of 14:54, 24 December 2014
Structure of a BRCA2-DSS1 complex
| |||||||||||
