1ec6
From Proteopedia
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CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN
Overview
The structure of a Nova protein K homology (KH) domain recognizing, single-stranded RNA has been determined at 2.4 A 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.
About this Structure
1EC6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome., Lewis HA, Musunuru K, Jensen KB, Edo C, Chen H, Darnell RB, Burley SK, Cell. 2000 Feb 4;100(3):323-32. PMID:10676814
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