Reactome | RPA associates with ssDNA in distinct complexes that can be ...

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created	[InstanceEdit:176246] D'Eustachio, P, 2006-03-03 16:44:08
dbId	176240
displayName	RPA associates with ssDNA in distinct complexes that can be ...
literatureReference	[LiteratureReference:176266] Human replication protein A binds single-stranded DNA in two distinct complexes [LiteratureReference:176103] Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA [LiteratureReference:69372] Replication protein A (RPA): the eukaryotic SSB.
schemaClass	Summation
text	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.

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