2RVC

Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase

Summary for 2RVC

• Entry DOI: 10.2210/pdb2rvc/pdb
• NMR Information: BMRB: 11595
• Descriptor: Interferon-inducible and double-stranded-dependent eIF-2kinase (1 entity in total)
• Functional Keywords: z dna binding protein, helix turn helix, dna binding protein
• Biological source: Carassius auratus (Goldfish)
• Total number of polymer chains: 1
• Total formula weight: 7458.51

Authors

Lee, A.,Park, C.,Park, J.,Kwon, M.,Choi, Y.,Kim, K.,Choi, B.,Lee, J. (deposition date: 2015-07-08, release date: 2016-02-03, Last modification date: 2024-05-01)

Primary citation

Lee, A.R.,Park, C.J.,Cheong, H.K.,Ryu, K.S.,Park, J.W.,Kwon, M.Y.,Lee, J.,Kim, K.K.,Choi, B.S.,Lee, J.H.
Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.
Nucleic Acids Res., 44:2936-2948, 2016

PubMed Abstract: Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune response and viral infection. Structural and biophysical studies show that ZBPs initially form an intermediate complex with B-DNA for B-Z conversion. However, a comprehensive understanding of the mechanism of Z-DNA binding and B-Z transition is still lacking, due to the absence of structural information on the intermediate complex. Here, we report the solution structure of the Zα domain of the ZBP-containing protein kinase from Carassius auratus(caZαPKZ). We quantitatively determined the binding affinity of caZαPKZ for both B-DNA and Z-DNA and characterized its B-Z transition activity, which is modulated by varying the salt concentration. Our results suggest that the intermediate complex formed by caZαPKZ and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform.

PubMed: 26792893
DOI: 10.1093/nar/gkw025

Experimental method

SOLUTION NMR