3sr2: Difference between revisions

Latest revision as of 16:05, 14 March 2024

Crystal Structure of Human XLF-XRCC4 ComplexCrystal Structure of Human XLF-XRCC4 Complex

Structural highlights

3sr2 is a 8 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 3.9708Å
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]

References

↑ 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
↑ 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
↑ 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
↑ 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

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OCA

[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

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3sr2 is ON HOLD
+==Crystal Structure of Human XLF-XRCC4 Complex==
+<StructureSection load='3sr2' size='340' side='right'caption='[[3sr2]], [[Resolution|resolution]] 3.97&Aring;' scene=''>
-Authors: Hammel, M., Classen, S., Tainer, J.A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3sr2]] is a 8 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=3SR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SR2 FirstGlance]. <br>
-Description: Crystal Structure of Human XLF-XRCC4 Complex
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9708&#8491;</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=3sr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sr2 OCA], [https://pdbe.org/3sr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sr2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sr2 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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Classen S]]
+[[Category: Hammel M]]
+[[Category: Tainer JA]]

3sr2: Difference between revisions

Latest revision as of 16:05, 14 March 2024

Crystal Structure of Human XLF-XRCC4 ComplexCrystal Structure of Human XLF-XRCC4 Complex

Structural highlights

Function

References

Contents

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3sr2: Difference between revisions

Latest revision as of 16:05, 14 March 2024

Crystal Structure of Human XLF-XRCC4 ComplexCrystal Structure of Human XLF-XRCC4 Complex

Structural highlights

Function

References

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