3ii6: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "3ii6" [edit=sysop:move=sysop]
No edit summary
 
(6 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3ii6.png|left|200px]]


{{STRUCTURE_3ii6|  PDB=3ii6  |  SCENE=  }}
==Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.==
 
<StructureSection load='3ii6' size='340' side='right'caption='[[3ii6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
===Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_19332554}}
</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>
 
<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>
==About this Structure==
<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>
[[3ii6]] is a 6 chain structure of [[DNA ligase]] with sequence 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].  
</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>


==See Also==
==See Also==
*[[DNA ligase|DNA ligase]]
*[[DNA ligase 3D structures|DNA ligase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019332554</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Junop, M.]]
[[Category: Large Structures]]
[[Category: Meesala, S.]]
[[Category: Junop M]]
[[Category: Atp-binding]]
[[Category: Meesala S]]
[[Category: Brct]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[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: Scid]]
[[Category: Xrcc4]]

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

Drag the structure with the mouse to rotate

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

OCA