5AWM
The Crystal Structure of JNK from Drosophila melanogaster Reveals an Evolutionarily Conserved Topology with that of Mammalian JNK Proteins.
Replaces: 4M3ASummary for 5AWM
| Entry DOI | 10.2210/pdb5awm/pdb |
| Descriptor | Stress-activated protein kinase JNK, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | c-jun n-terminal kinase, map kinase, drosophila jnk pathway, transferase |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 46064.35 |
| Authors | Boonserm, P. (deposition date: 2015-07-06, release date: 2015-08-05, Last modification date: 2025-03-19) |
| Primary citation | Chimnaronk, S.,Sitthiroongruang, J.,Srisucharitpanit, K.,Srisaisup, M.,Ketterman, A.J.,Boonserm, P. The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins. Bmc Struct.Biol., 15:17-17, 2015 Cited by PubMed Abstract: 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. PubMed: 26377800DOI: 10.1186/s12900-015-0045-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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