PUBLICATION
Structural and functional studies of a large winged Z-DNA binding domain of Danio rerio protein kinase PKZ
- Authors
- Subramani, V.K., Kim, D., Yun, K., Kim, K.K.
- ID
- ZDB-PUB-160608-5
- Date
- 2016
- Source
- FEBS letters 590(14): 2275-85 (Journal)
- Registered Authors
- Keywords
- B-Z transition, PKZ, Z-DNA, Zebrafish, Z?
- MeSH Terms
-
- Animals
- Zebrafish*
- Crystallography, X-Ray
- Mutation
- Structure-Activity Relationship
- Protein Structure, Secondary
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- DNA, Z-Form/chemistry
- DNA, Z-Form/genetics
- DNA, Z-Form/metabolism
- Protein Kinases/chemistry*
- Protein Kinases/genetics
- Protein Kinases/metabolism
- PubMed
- 27265117 Full text @ FEBS Lett.
Citation
Subramani, V.K., Kim, D., Yun, K., Kim, K.K. (2016) Structural and functional studies of a large winged Z-DNA binding domain of Danio rerio protein kinase PKZ. FEBS letters. 590(14):2275-85.
Abstract
The Z-DNA binding domain of PKZ from zebrafish (Danio rerio; drZαPKZ ) contains the largest β-wing among known Z-DNA binding domains. To elucidate the functional implication of the β-wing, we solved the crystal structure of apo-drZαPKZ . Structural comparison with its Z-DNA-bound form revealed a large conformational change within the β-wing during Z-DNA binding. Biochemical studies of protein mutants revealed that two basic residues in the β-wing are responsible for Z-DNA recognition as well as fast B-Z transition. Therefore, the extra basic residues in the β-wing of drZαPKZ are necessary for the fast B-Z transition activity. This article is protected by copyright. All rights reserved.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping