Title : Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide.

Pub. Date : 1996 Jan 30

PMID : 8573568






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive. Ribose eukaryotic translation elongation factor 2 Homo sapiens
2 Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive. Ribose eukaryotic translation elongation factor 2 Homo sapiens
3 Residues 39-46 of the active-site loop of the C-domain become disordered upon NAD binding, suggesting a potential role for this loop in the recognition of the ADP-ribose acceptor substrate, EF-2. Ribose eukaryotic translation elongation factor 2 Homo sapiens