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Literature summary for 6.5.1.1 extracted from

  • Wu, P.Y.; Frit, P.; Meesala, S.; Dauvillier, S.; Modesti, M.; Andres, S.N.; Huang, Y.; Sekiguchi, J.; Calsou, P.; Salles, B.; Junop, M.S.
    Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4 (2009), Mol. Cell. Biol., 29, 3163-3172.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
LigIV in complex with XRCC4 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
Homo sapiens
-
MRC5-SV cell
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
DNA ligase IV
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens

Expression

Organism Comment Expression
Homo sapiens ectopic overexpression of competing LigIV fragments downregulates endogenous LigIV protein down

General Information

General Information Comment Organism
physiological function the XRCC4/DNA ligase IV complex catalyzes the final ligation step in nonhomologous end-joining Homo sapiens