RPA complexed to ssDNA [nucleoplasm]

Stable Identifier
Homo sapiens
RPA-ssDNA complex
Locations in the PathwayBrowser
RPA associates with ssDNA in distinct complexes that can be distinguished by the length of ssDNA occluded by each RPA molecule. These complexes reflect the progressive association of distinct DNA-binding domains present in the RPA heterotrimeric structure. Binding is coupled to significant conformational changes within RPA that are observable at the microscopic level. Presumably, the different conformations of free and ssDNA-bound RPA allow the protein to selectively interact with factors such as ATR-ATRIP when bound to DNA.
Literature References
PubMed ID Title Journal Year
11157767 Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding

Bochkareva, E, Bochkarev, A, Belegu, V, Korolev, S

EMBO J 2001
10473346 Replication protein A (RPA): the eukaryotic SSB.

Daniely, Y, Borowiec, JA, Iftode, C

Crit Rev Biochem Mol Biol 1999
8196638 Human replication protein A binds single-stranded DNA in two distinct complexes

Borowiec, JA, Blackwell, LJ

Mol Cell Biol 1994
11927569 Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA

Bochkareva, E, Bochkarev, A, Lees-Miller, SP, Korolev, S

EMBO J 2002
Inferred To
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