5EKN

Crystal structure of MAPK13 complex with inhibitor

Summary for 5EKN

• Entry DOI: 10.2210/pdb5ekn/pdb
• Related: 4EYJ 4EYM 4MYG 4YNO 5EKO
• Descriptor: Mitogen-activated protein kinase 13, 1-(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)-3-[4-(pyridin-4-ylsulfanyl)phenyl]urea (3 entities in total)
• Functional Keywords: kinase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 43015.39

Authors

Brett, T.J.,Miller, C.A.,Yurtsever, Z. (deposition date: 2015-11-03, release date: 2016-07-06, Last modification date: 2023-09-27)

Primary citation

Yurtsever, Z.,Patel, D.A.,Kober, D.L.,Su, A.,Miller, C.A.,Romero, A.G.,Holtzman, M.J.,Brett, T.J.
First comprehensive structural and biophysical analysis of MAPK13 inhibitors targeting DFG-in and DFG-out binding modes.
Biochim.Biophys.Acta, 1860:2335-2344, 2016

PubMed Abstract: P38 MAP kinases are centrally involved in mediating extracellular signaling in various diseases. While much attention has previously been focused on the ubiquitously expressed family member MAPK14 (p38α), recent studies indicate that family members such as MAPK13 (p38δ) display a more selective cellular and tissue expression and might therefore represent a specific kinase to target in certain diseases.

PubMed: 27369736
DOI: 10.1016/j.bbagen.2016.06.023

Experimental method

X-RAY DIFFRACTION (2.594 Å)