NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA.
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ABSTRACT:
SUBMITTER: Brosey CA
PROVIDER: S-EPMC2711642 | biostudies-literature | 2009 May
REPOSITORIES: biostudies-literature
Publications
NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA.
Brosey Chris A CA Chagot Marie-Eve ME Ehrhardt Mark M Pretto Dalyir I DI Weiner Brian E BE Chazin Walter J WJ
Journal of the American Chemical Society 20090501 18
Modular proteins with multiple domains tethered by flexible linkers have variable global architectures. Using the eukaryotic ssDNA binding protein, Replication Protein A (RPA), we demonstrate that NMR spectroscopy is a powerful tool to characterize the remodeling of architecture in different functional states. The first direct evidence is obtained for the remodeling of RPA upon binding ssDNA, including an alteration in the availability of the RPA32N domain that may help explain its damage-depend ...[more]
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