1DT4

CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN

Summary for 1DT4

• Entry DOI: 10.2210/pdb1dt4/pdb
• Related: 1DTJ 1EC6
• Descriptor: NEURO-ONCOLOGICAL VENTRAL ANTIGEN 1 (1 entity in total)
• Functional Keywords: kh domain, alpha-beta fold, rna-binding motif, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 7895.20

Authors

Lewis, H.A.,Chen, H.,Edo, C.,Buckanovich, R.J.,Yang, Y.Y.L. (deposition date: 2000-01-11, release date: 2000-02-11, Last modification date: 2024-02-07)

Primary citation

Lewis, H.A.,Chen, H.,Edo, C.,Buckanovich, R.J.,Yang, Y.Y.,Musunuru, K.,Zhong, R.,Darnell, R.B.,Burley, S.K.
Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains.
Structure Fold.Des., 7:191-203, 1999

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.

PubMed: 10368286
DOI: 10.1016/S0969-2126(99)80025-2

Experimental method

X-RAY DIFFRACTION (2.6 Å)