2l6l | pdb_00002l6l
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Solution structure of human J-protein co-chaperone, Dph4
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Structural highlights
FunctionDJC24_HUMAN Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron-bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta).[1] [2] See AlsoReferences
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This page was last modified 06:53, 1 May 2024.