3NZ0
Non-phosphorylated TYK2 kinase with CMP6
Summary for 3NZ0
| Entry DOI | 10.2210/pdb3nz0/pdb |
| Related | 3NYX |
| Descriptor | Non-receptor tyrosine-protein kinase TYK2, 2-TERT-BUTYL-9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-IMIDAZ[4,5-F]ISOQUINOLINE-7-ONE (3 entities in total) |
| Functional Keywords | protein kinase, tyrosine phosphorylation, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 35295.40 |
| Authors | Eigenbrot, C.,Ultsch, M. (deposition date: 2010-07-15, release date: 2010-10-20, Last modification date: 2023-09-06) |
| Primary citation | Tsui, V.,Gibbons, P.,Ultsch, M.,Mortara, K.,Chang, C.,Blair, W.,Pulk, R.,Stanley, M.,Starovasnik, M.,Williams, D.,Lamers, M.,Leonard, P.,Magnuson, S.,Liang, J.,Eigenbrot, C. A new regulatory switch in a JAK protein kinase. Proteins, 79:393-401, 2011 Cited by PubMed Abstract: Members of the JAK family of protein kinases mediate signal transduction from cytokine receptors to transcription factor activation. Over-stimulation of these pathways is causative in immune disorders like rheumatoid arthritis, psoriasis, lupus, and Crohn's disease. A search for selective inhibitors of a JAK kinase has led to our characterization of a previously unknown kinase conformation arising from presentation of Tyr962 of TYK2 to an inhibitory small molecule via an H-bonding interaction. A small minority of protein kinase domains has a Tyrosine residue in this position within the αC-β4 loop, and it is the only amino acid commonly seen here with H-bonding potential. These discoveries will aid design of inhibitors that discriminate among the JAK family and more widely among protein kinases. PubMed: 21117080DOI: 10.1002/prot.22889 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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