title: Movement and specificity in a modular DNA binding protein.
abstract: The single-stranded DNA (ssDNA) binding protein RPA binds to and protects ssDNA while simultaneously recruiting numerous replication and repair proteins essential for genome integrity. In this issue of Structure, Brosey et al. (2015) show that the flexibility and interactions of the modular domains of RPA are altered by ssDNA binding and suggest that these changes in configurational freedom are important for the many functions of RPA.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
authors.forename: Cary
authors.initials: C
authors.lastname: Liptak
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA; Department of Chemistry, Yale University, New Haven, CT 06520, USA. Electronic address: patrick.loria@yale.edu.
authors.forename: J Patrick
authors.initials: JP
authors.lastname: Loria
mesh_terms: D004247:DNA / Q000378:metabolism*; D008958:Models, Molecular; D051716:Replication Protein A / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D051716:Replication Protein A; D004247:DNA