1DPU

SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)

Summary for 1DPU

• Entry DOI: 10.2210/pdb1dpu/pdb
• Descriptor: REPLICATION PROTEIN A (RPA32) C-TERMINAL DOMAIN, URACIL DNA GLYCOSYLASE (UNG2) (2 entities in total)
• Functional Keywords: protein-peptide complex, dna repair, dna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P15927; Isoform 1: Mitochondrion. Isoform 2: Nucleus: P13051
• Total number of polymer chains: 2
• Total formula weight: 12411.88

Authors

Mer, G.,Edwards, A.M.,Chazin, W.J. (deposition date: 1999-12-27, release date: 2000-11-10, Last modification date: 2024-05-22)

Primary citation

Mer, G.,Bochkarev, A.,Gupta, R.,Bochkareva, E.,Frappier, L.,Ingles, C.J.,Edwards, A.M.,Chazin, W.J.
Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.
Cell(Cambridge,Mass.), 103:449-456, 2000

PubMed Abstract: Replication protein A (RPA), the nuclear ssDNA-binding protein in eukaryotes, is essential to DNA replication, recombination, and repair. We have shown that a globular domain at the C terminus of subunit RPA32 contains a specific surface that interacts in a similar manner with the DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which functions in a different repair pathway. NMR structures of the RPA32 domain, free and in complex with the minimal interaction domain of UNG2, were determined, defining a common structural basis for linking RPA to the nucleotide excision, base excision, and recombinational pathways of repairing damaged DNA. Our findings support a hand-off model for the assembly and coordination of different components of the DNA repair machinery.

PubMed: 11081631
DOI: 10.1016/S0092-8674(00)00136-7

Experimental method

SOLUTION NMR