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dc.contributor.authorSarin Chimnaronken_US
dc.contributor.authorJatuporn Sitthiroongruangen_US
dc.contributor.authorKanokporn Srisucharitpaniten_US
dc.contributor.authorMonrudee Srisaisupen_US
dc.contributor.authorAlbert J. Kettermanen_US
dc.contributor.authorPanadda Boonsermen_US
dc.contributor.otherMahidol University. Institute of Molecular Biosciencesen_US
dc.date.accessioned2017-08-23T07:37:37Z-
dc.date.available2017-08-23T07:37:37Z-
dc.date.created2017-08-23-
dc.date.issued2015-
dc.identifier.citationBMC Structural Biology. Vol.15, (2015), 17en_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/2763-
dc.description.abstractBackground: 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.en_US
dc.language.isoenen_US
dc.rightsMahidol Universityen_US
dc.subjectcrystal structureen_US
dc.subjectJNKen_US
dc.subjectDrosophilaen_US
dc.subjectOpen Access articleen_US
dc.titleThe crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteinsen_US
dc.typeArticleen_US
dc.rights.holderBioMed Centralen_US
dc.identifier.doi10.1186/s12900-015-0045-1-
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