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Figure 2

 

p38 MAPK14, with the α helices in pink, and the β strands in yellow. Human p38 MAPK14 contains 20 α helices of total length of 139 residues,13 β strands (58 residues) and 8 turns (24 residues).

 

 

p38 MAPK14 consists of a, conserved for all MAPKs, TXY motif, located in the activation loop at position 180-182, pictured here in green colour. For p38 MAPK

This motif possesses threonine (180) and tyrosine (182) residues, both of which get phosphorylated, so that kinase domain is locked in a catalytically competent conformation. Characteristically for the p38 class of MAPKs, ‘X’ residue in this motif is glycine at residue 181.

 

© 2016 by CELL2007/8 Group 8, UCL.

Proudly produced by Alvin Chu, Nancy Ellis, Lily Gates, Vaughn Lewis, Michael Moore, Michael Sewell, Macro Spaeth and Cyprian Winogradow 

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