1miu: Difference between revisions

No edit summary
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1miu.gif|left|200px]]


{{Structure
==Structure of a BRCA2-DSS1 complex==
|PDB= 1miu |SIZE=350|CAPTION= <scene name='initialview01'>1miu</scene>, resolution 3.1&Aring;
<StructureSection load='1miu' size='340' side='right'caption='[[1miu]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<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.ebi.ac.uk/pdbsum/1miu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1miu RCSB]</span>
== Disease ==
}}
[https://www.uniprot.org/uniprot/SEM1_HUMAN SEM1_HUMAN] Split hand-split foot malformation.
== Function ==
[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>
    <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/main_output.php?pdb_ID=1miu ConSurf].
<div style="clear:both"></div>


'''Structure of a BRCA2-DSS1 complex'''
==See Also==
 
*[[BRCA 3D structures|BRCA 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1MIU is a [[Protein complex]] structure of sequences 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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12228710 12228710]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Chen, P L.]]
[[Category: RecA and Rad51]]
[[Category: Jeffrey, P D.]]
[[Category: Chen PL]]
[[Category: Kinnucan, E.]]
[[Category: Jeffrey PD]]
[[Category: Lee, W H.]]
[[Category: Kinnucan E]]
[[Category: Miller, J.]]
[[Category: Lee WH]]
[[Category: Pavletich, N P.]]
[[Category: Miller J]]
[[Category: Sun, Y.]]
[[Category: Pavletich NP]]
[[Category: Thoma, N H.]]
[[Category: Sun Y]]
[[Category: Yang, H.]]
[[Category: Thoma NH]]
[[Category: Zheng, N.]]
[[Category: Yang H]]
[[Category: breast cancer susceptibility]]
[[Category: Zheng N]]
[[Category: dna-binding]]
[[Category: tumor suppressor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:39 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA