@article{
author = "Lee, Yu-Ming and Babu, C. Satheesan and Chen, Yao Chi and Milčić, Miloš K. and Qu, Yuanyuan and Lim, Carmay",
year = "2010",
abstract = "The ADP-ribosylating toxins (ADPRTs) and poly(ADP-ribose) polymerases (PARPs) are two important drug target protein families. Although the Y-X(10)-Y motif for the diphtheria toxin group and the STS motif for the other ADPRTs have been found to recognize the NAD(+) substrate, it is not known (i) if these two different motifs share any structural similarity, (ii) the key forces/residues contributing to NAD(+) binding, and (iii) if they recognize the same or different NAD(+) conformations. Here, we show that even though the different toxin groups and PARPs share insignificant sequence identity, they share a similar 3D structure shaped like a scorpion (the "scorpion" motif) whose first three and last residues interact mainly with the NAD(+) nicotinamide ring via van der Waals forces. This locally conserved structure binds the nicotinamide mononucleotide moiety in a structurally conserved ringlike conformation. The biological implications/applications of locally conserved structures for toxins/PARPs and the nicotinamide mononucleotide are discussed.",
publisher = "Amer Chemical Soc, Washington",
journal = "Journal of Medicinal Chemistry",
title = "Conserved Structural Motif for Recognizing Nicotinamide Adenine Dinucleotide in Poly(ADP-ribose) Polymerases and ADP-Ribosylating Toxins: Implications for Structure-Based Drug Design",
volume = "53",
number = "10",
pages = "4038-4049",
doi = "10.1021/jm1001106"
}