3NNU: Crystal structure of P38 alpha in complex with DP1376

Citation:
Abstract
Switch control pocket inhibitors of p38-alpha kinase are described. Durable type II inhibitors were designed which bind to arginines (Arg67 or Arg70) that function as key residues for mediating phospho-threonine 180 dependant conformational fluxing of p38-alpha from an inactive type II state to an active type I state. Binding to Arg70 in particular led to potent inhibitors, exemplified by DP-802, which also exhibited high kinase selectivity. Binding to Arg70 obviated the requirement for binding into the ATP Hinge region. X-ray crystallography revealed that DP-802 and analogs induce an enhanced type II conformation upon binding to either the unphosphorylated or the doubly phosphorylated form of p38-alpha kinase.
PDB ID: 3NNUDownload
MMDB ID: 84853
PDB Deposition Date: 2010/6/24
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 3NNU: monomeric; determined by author and by software (PISA)
Molecular Components in 3NNU
Label Count Molecule
Protein (1 molecule)
1
Mitogen-activated Protein Kinase 14(Gene symbol: MAPK14)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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