UV excision repair protein

Function UV excision repair protein (Rad23) is a yeast protein involved in nucleotide excision repair. The human homologs are hHR23A and hHR23B. hHR23A plays a role in translocating polyubiquitinated proteins to the proteasome. Structural highlights The protein contains a modular domain structure consisting of ubiquitin-like domain, ubiquitin-associated domain and XPC(xeroderma pigmentosum group C protein)-binding domain.

spinqualitylabelsall models Structure of yeast Rad23 (green) complex with Rad4 (grey) (PDB entry 2qsf) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structures of UV excision repair protein3D Structures of UV excision repair protein

Updated on 24-March-2020

{"openlevels":0}

• Rad23; Domains - UBL 1-78; XPC-binding 239-398
  • 2nbu – yRad23 UBL domain – yeast - NMR
    
  • 2qsf – yRad23 XPC-binding domain + Rad4
    
  • 2qsg, 2qsh, 4yir, 6cfi – yRad23 XPC-binding domain + Rad4 + DNA
    
  • 1x3w, 3esw – yRad23 XPC-binding domain + peptide:N-glycanase
    
  • 1x3z – yRad23 XPC-binding domain + peptide:N-glycanase + peptide
    
  • 2nbw – yRad23 UBL domain + RPN1 - NMR
    
  • 3m62 – yRad23 UBL domain + Ufd2
    
• Rad23 homolog hHR23 A; Domains: UBA 156-204; XPC-binding 223-317
  • 1oqy, 1qze – hHR23A – human - NMR
    
  • 1f4i – hHR23A C-terminal domain (mutant) - NMR
    
  • 1ify – hHR23A internal UBA domain - NMR
    
  • 5xbo – hHR23A internal UBA domain + ubiquitin - NMR
    
  • 1p98, 2wyq – hHR23A UBA domain - NMR
    
  • 1p9d – hHR23A UBA domain + S5a - NMR
    
  • 5xbo – hHR23A UBA domain + ubiquitin - NMR
    
  • 1tp4 – hHR23A XPC-binding domain - NMR
    
• Rad23 homolog hHR23 B
  • 1p1a – hHR23B UBA domain - NMR
    
  • 1pve – hHR23B XPC-binding domain - NMR
    
  • 1uel – hHR23B UBA domain + S5a - NMR
    
  • 1x3w, 2f4m – HR23B XPC-binding domain + peptide:N-glycanase - mouse