1Z1D
Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.
Summary for 1Z1D
| Entry DOI | 10.2210/pdb1z1d/pdb |
| Related | 1DPU 1TBD |
| Descriptor | Replication protein A 32 kDa subunit, Large T antigen (2 entities in total) |
| Functional Keywords | winged helix-turn-helix motif, origin binding domain, protein-protein complex, replication |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P15927 Host nucleus: P03070 |
| Total number of polymer chains | 2 |
| Total formula weight | 26110.49 |
| Authors | Arunkumar, A.I.,Klimovich, V.,Jiang, X.,Ott, R.D.,Mizoue, L.,Fanning, E.,Chazin, W.J. (deposition date: 2005-03-03, release date: 2005-05-17, Last modification date: 2024-05-22) |
| Primary citation | Arunkumar, A.I.,Klimovich, V.,Jiang, X.,Ott, R.D.,Mizoue, L.,Fanning, E.,Chazin, W.J. Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome. Nat.Struct.Mol.Biol., 12:332-339, 2005 Cited by PubMed Abstract: Simian virus 40 (SV40) provides a model system for the study of eukaryotic DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40 replication requires interaction of Tag with the host single-stranded DNA-binding protein, replication protein A (hRPA). The C-terminal domain of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but whether it interacts with Tag is not known. Affinity chromatography and NMR revealed physical interaction between hRPA32C and the Tag origin DNA-binding domain, and a structural model of the complex was determined. Point mutations were then designed to reverse charges in the binding sites, resulting in substantially reduced binding affinity. Corresponding mutations introduced into intact hRPA impaired initiation of replication and primosome activity, implying that this interaction has a critical role in assembly and progression of the SV40 replisome. PubMed: 15793585DOI: 10.1038/nsmb916 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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