T antigen origin binding domain in complex with RPA32 C-terminal domain

DNA replication, recombination and repair

Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome.

Solution Structure Of The C-Terminal Domain Of Human Rpa32 Complexed With Ung2(73-88)

Structural Model For The Interaction Between Rpa32 C- Terminal Domain And Sv40 T Antigen Origin Binding Domain

Full-Length Replication Protein A Subunits Rpa14 And Rpa32

Crystal Structure Of Full-Length Human Rpa1432 HETERODIMER

Crystal Complex Of Rpa32c And Smarcal1 N-terminus

replication protein A2, 32kDa [synthetic construct]

Replication protein A2, 32kDa [Homo sapiens]

replication protein A 32 kDa subunit [Pongo abelii]

replication protein A 32 kDa subunit [Sus scrofa]

replication protein A 32 kDa subunit [Macaca mulatta]

replication protein A 32 kDa subunit isoform 2 [Homo sapiens]

replication protein A 32 kDa subunit isoform 3 [Homo sapiens]

RecName: Full=Replication protein A 32 kDa subunit; Short=RP-A p32; AltName: Full=Replication factor A protein 2; Short=RF-A pr

'Backbone 1H and 15N Chemical Shift Assignments for T antigen origin binding domain in the presence of RPA32C'

Rigid body docking, Semi-flexible simulated annealing, Refinement using explicit water
Sequence-specific 1H, 13C, and 15N Resonance Assignment of Tag-OBD
Structural analysis of the interaction between RPA32C and Tag-OBD