3ii6: Difference between revisions

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==Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.==
The line below this paragraph, containing "STRUCTURE_3ii6", creates the "Structure Box" on the page.
<StructureSection load='3ii6' size='340' side='right'caption='[[3ii6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3ii6]] is a 6 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=3II6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3II6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
{{STRUCTURE_3ii6| PDB=3ii6 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ii6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ii6 OCA], [https://pdbe.org/3ii6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ii6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ii6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ii6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XRCC4_HUMAN XRCC4_HUMAN] Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.<ref>PMID:8548796</ref> <ref>PMID:10854421</ref> <ref>PMID:10757784</ref> <ref>PMID:16412978</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/ii/3ii6_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=3ii6 ConSurf].
<div style="clear:both"></div>


===Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.===
==See Also==
 
*[[DNA ligase 3D structures|DNA ligase 3D structures]]
 
== References ==
==Disease==
<references/>
Known disease associated with this structure: LIG4 syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601837 601837]], Multiple myeloma, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601837 601837]]
__TOC__
 
</StructureSection>
==About this Structure==
3II6 is a 6 chains structure of 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=3II6 OCA].
 
==Reference==
<ref group="xtra">PMID:19332554</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Junop, M.]]
[[Category: Large Structures]]
[[Category: Meesala, S.]]
[[Category: Junop M]]
[[Category: Alternative splicing]]
[[Category: Meesala S]]
[[Category: Atp-binding]]
[[Category: Brct]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Coiled coil]]
[[Category: Disease mutation]]
[[Category: Dna damage]]
[[Category: Dna ligase iv]]
[[Category: Dna recombination]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Isopeptide bond]]
[[Category: Ligase]]
[[Category: Ligase/dna binding protein complex]]
[[Category: Magnesium]]
[[Category: Metal-binding]]
[[Category: Nhej]]
[[Category: Nucleotide-binding]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Scid]]
[[Category: Ubl conjugation]]
[[Category: Xrcc4]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 12 12:43:59 2009''

Latest revision as of 13:05, 21 February 2024

Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.

Structural highlights

3ii6 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

XRCC4_HUMAN Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Li Z, Otevrel T, Gao Y, Cheng HL, Seed B, Stamato TD, Taccioli GE, Alt FW. The XRCC4 gene encodes a novel protein involved in DNA double-strand break repair and V(D)J recombination. Cell. 1995 Dec 29;83(7):1079-89. PMID:8548796
  2. ↑ Chen L, Trujillo K, Sung P, Tomkinson AE. Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem. 2000 Aug 25;275(34):26196-205. PMID:10854421 doi:10.1074/jbc.M000491200
  3. ↑ Nick McElhinny SA, Snowden CM, McCarville J, Ramsden DA. Ku recruits the XRCC4-ligase IV complex to DNA ends. Mol Cell Biol. 2000 May;20(9):2996-3003. PMID:10757784
  4. ↑ Foster RE, Nnakwe C, Woo L, Frank KM. Monoubiquitination of the nonhomologous end joining protein XRCC4. Biochem Biophys Res Commun. 2006 Mar 3;341(1):175-83. Epub 2006 Jan 6. PMID:16412978 doi:S0006-291X(05)02903-7

3ii6, resolution 2.40Å

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