XPC/hHR23B heterodimer

initiates global genome nucleotide excision repair by binding to lesion, distorting DNA double helix & recruiting other factors. possible role in open complex formation/stabilization. hHR23A can substitute for hHR23B in vitro.

General

endodeoxyribonuclease molecular complex

Properties

MOTIF: active site SUBUNITS: UV excision repair protein RAD23 homolog B COMPARTMENT: cytoplasm cell nucleus MOTIF: ubiquitin domain {1-80} threonine-rich region {103-106} MOTIF: threonine residue (SEVERAL) Thr phosphorylation site {T155} Ser phosphorylation site {S160} UBA domain {178-232} alanine-rich region {254-260} MOTIF: alanine residue (SEVERAL) threonine-rich region {261-269} MOTIF: threonine residue (SEVERAL) STI1 {274-317} binding site SITE: 275-332 EFFECTOR-BOUND: DNA repair protein complementing XP-C cells BOUND-VIA: binding site glycine-rich region {336-348} UBA domain {357-409} DNA repair protein complementing XP-C cells COMPARTMENT: cell nucleus MOTIF: binding site EFFECTOR-BOUND: UV excision repair protein RAD23 homolog B BOUND-VIA: binding site

References

- de Laat WL et al, Molecular mechonisms of nucleotide excision repair. Genes & Dev 13:768-85, 1999 PMID: 10197977

Components

DNA repair protein complementing XP-C cells; xeroderma pigmentosum group C-complementing protein; p125 (XPC, XPCC) UV excision repair protein RAD23 homolog B; HR23B; hHR23B; XP-C repair-complementing complex 58 kD protein; p58 (RAD23B)