Journal
CELL
Volume 100, Issue 3, Pages 323-332Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(00)80668-6
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- NIGMS NIH HHS [GM07739] Funding Source: Medline
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The structure of a Nova protein K homology (KH) domain recognizing single-stranded RNA has been determined at 2.4 Angstrom resolution. Mammalian Nova antigens (1 and 2) constitute an important family of regulators of RNA metabolism in neurons, first identified using sera from cancer patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus ataxia (POMA). The structure of the third KH domain (KH3) of Nova-2 bound to a stem loop RNA resembles a molecular vise, with 5'-Ura-Cyt-Ade-Cyt-3' pinioned between an invariant Gly-X-X-Gly motif and the variable loop. Tetranucleotide recognition is supported by an aliphatic alpha helix/beta sheet RNA-binding platform, which mimics 5'-Ura-Gua-3' by making Watson-Crick-like hydrogen bonds with 5'-Cyt-Ade-3'. Sequence conservation suggests that fragile X mental retardation results from perturbation of RNA binding by the FMR1 protein.
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