Download MendeleyCrystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains.
Lewis, H.A., Chen, H., Edo, C., Buckanovich, R.J., Yang, Y.Y., Musunuru, K., Zhong, R., Darnell, R.B., Burley, S.K.(1999) Structure 7: 191-203
- PubMed: 10368286
- DOI: https://doi.org/10.1016/S0969-2126(99)80025-2
- Primary Citation of Related Structures:
1DT4, 1DTJ - PubMed Abstract:
Nova-1 and Nova-2 are related neuronal proteins that were initially cloned using antisera obtained from patients with the autoimmune neurological disease paraneoplastic opsoclonus-myoclonus ataxia (POMA). Both of these disease gene products contain three RNA-binding motifs known as K-homology or KH domains, and their RNA ligands have been identified via binding-site selection experiments. The KH motif structure has been determined previously using NMR spectroscopy, but not using X-ray crystallography. Many proteins contain more than one KH domain, yet there is no published structural information regarding the behavior of such multimers.
Organizational Affiliation:
Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY, 10021 USA.
