5awm | pdb_00005awm
The Crystal Structure of JNK from Drosophila melanogaster Reveals an Evolutionarily Conserved Topology with that of Mammalian JNK Proteins.
Structural highlights
FunctionJNK_DROME Responds to activation by environmental stress by phosphorylating a number of transcription factors, primarily components of AP-1 such as Jra and also the transcriptional repressor aop, and thus regulates transcriptional activity. Component of the immune response activated by bacterial infection, and is involved in wound healing and in dorsal closure, a morphogenetic movement during embryogenesis. Controls the expression of a phosphatase, puckered, at the edges of wounded epidermal tissue and in the dorsal epithelium during dorsal closure.[1] [2] [3] [4] Publication Abstract from PubMedBACKGROUND: 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 A 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. The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins.,Chimnaronk S, Sitthiroongruang J, Srisucharitpanit K, Srisaisup M, Ketterman AJ, Boonserm P BMC Struct Biol. 2015 Sep 16;15:17. doi: 10.1186/s12900-015-0045-1. PMID:26377800[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
