1EC6

CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN

Summary for 1EC6

• Entry DOI: 10.2210/pdb1ec6/pdb
• Descriptor: 20-MER RNA HAIRPIN, RNA-BINDING PROTEIN NOVA-2 (3 entities in total)
• Functional Keywords: kh domain, alpha-beta fold, rna-binding motif, protein/rna structure, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 31559.36

Authors

Lewis, H.A.,Musunuru, K.,Jensen, K.B.,Edo, C.,Chen, H. (deposition date: 2000-01-25, release date: 2000-02-21, Last modification date: 2024-02-07)

Primary citation

Lewis, H.A.,Musunuru, K.,Jensen, K.B.,Edo, C.,Chen, H.,Darnell, R.B.,Burley, S.K.
Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome.
Cell(Cambridge,Mass.), 100:323-332, 2000

PubMed Abstract: 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.

PubMed: 10676814
DOI: 10.1016/S0092-8674(00)80668-6

Experimental method

X-RAY DIFFRACTION (2.4 Å)