Ontology highlight
ABSTRACT:
SUBMITTER: Song J
PROVIDER: S-EPMC2563106 | biostudies-literature | 2008 Oct
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20080929 40
We identified a functional domain (XlePABP2-TRP) of Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2). The NMR structure of XlePABP2-TRP revealed that the protein is a homodimer formed by the antiparallel association of beta-strands from the single RNA recognition motif (RRM) domain of each subunit. In each subunit of the homodimer, the canonical RNA recognition site is occluded by a polyproline motif. Upon poly(A) binding, XlePABP2-TRP undergoes a dimer-monomer transition that ...[more]