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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/35381
Title: The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins
Authors: Sarin Chimnaronk
Jatuporn Sitthiroongruang
Kanokporn Srisucharitpanit
Monrudee Srisaisup
Albert J. Ketterman
Panadda Boonserm
Mahidol University
Burapha University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 16-Sep-2015
Citation: BMC Structural Biology. Vol.15, No.1 (2015)
Abstract: © 2015 Chimnaronk et al. Background: The c-Jun N-terminal kinases (JNKs), members of the mitogen-activated protein kinase (MAPK) family, engage in diverse cellular responses to signals produced under normal development and stress conditions. In Drosophila, only one JNK member is present, whereas ten isoforms from three JNK genes (JNK1, 2, and 3) are present in mammalian cells. To date, several mammalian JNK structures have been determined, however, there has been no report of any insect JNK structure. Results: We report the first structure of JNK from Drosophila melanogaster (DJNK). The crystal structure of the unphosphorylated form of DJNK complexed with adenylyl imidodiphosphate (AMP-PNP) has been solved at 1.79 Å resolution. The fold and topology of DJNK are similar to those of mammalian JNK isoforms, demonstrating their evolutionarily conserved structures and functions. Structural comparisons of DJNK and the closely related mammalian JNKs also allow identification of putative catalytic residues, substrate-binding sites and conformational alterations upon docking interaction with Drosophila scaffold proteins. Conclusions: The DJNK structure reveals common features with those of the mammalian JNK isoforms, thereby allowing the mapping of putative catalytic and substrate binding sites. Additionally, structural changes upon peptide binding could be predicted based on the comparison with the closely-related JNK3 structure in complex with pepJIP1. This is the first structure of insect JNK reported to date, and will provide a platform for future mutational studies in Drosophila to ascertain the functional role of insect JNK.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84941620956&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/35381
ISSN: 14726807
Appears in Collections:Scopus 2011-2015

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