Ontology highlight
ABSTRACT:
SUBMITTER: Bochkareva E
PROVIDER: S-EPMC125950 | biostudies-literature | 2002 Apr
REPOSITORIES: biostudies-literature
Bochkareva Elena E Korolev Sergey S Lees-Miller Susan P SP Bochkarev Alexey A
The EMBO journal 20020401 7
The human single-stranded DNA-binding protein, replication protein A (RPA) binds DNA in at least two different modes: initial [8-10 nucleotides (nt)] and stable ( approximately 30 nt). Switching from 8 to 30 nt mode is associated with a large conformational change. Here we report the 2.8 A structure of the RPA trimerization core comprising the C-terminal DNA-binding domain of subunit RPA70 (DBD-C), the central DNA-binding domain of subunit RPA32 (DBD-D) and the entire RPA14 subunit. All three do ...[more]