TY  - JOUR
AU  - Lee, Yu-Ming
AU  - Babu, C. Satheesan
AU  - Chen, Yao Chi
AU  - Milčić, Miloš K.
AU  - Qu, Yuanyuan
AU  - Lim, Carmay
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1080
AB  - 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.
PB  - Amer Chemical Soc, Washington
T2  - Journal of Medicinal Chemistry
T1  - Conserved Structural Motif for Recognizing Nicotinamide Adenine Dinucleotide in Poly(ADP-ribose) Polymerases and ADP-Ribosylating Toxins: Implications for Structure-Based Drug Design
VL  - 53
IS  - 10
SP  - 4038
EP  - 4049
DO  - 10.1021/jm1001106
ER  - 

@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"
}

Lee, Y., Babu, C. S., Chen, Y. C., Milčić, M. K., Qu, Y.,& Lim, C.. (2010). Conserved Structural Motif for Recognizing Nicotinamide Adenine Dinucleotide in Poly(ADP-ribose) Polymerases and ADP-Ribosylating Toxins: Implications for Structure-Based Drug Design. in Journal of Medicinal Chemistry
Amer Chemical Soc, Washington., 53(10), 4038-4049.
https://doi.org/10.1021/jm1001106

Lee Y, Babu CS, Chen YC, Milčić MK, Qu Y, Lim C. Conserved Structural Motif for Recognizing Nicotinamide Adenine Dinucleotide in Poly(ADP-ribose) Polymerases and ADP-Ribosylating Toxins: Implications for Structure-Based Drug Design. in Journal of Medicinal Chemistry. 2010;53(10):4038-4049.
doi:10.1021/jm1001106 .

Lee, Yu-Ming, Babu, C. Satheesan, Chen, Yao Chi, Milčić, Miloš K., Qu, Yuanyuan, Lim, Carmay, "Conserved Structural Motif for Recognizing Nicotinamide Adenine Dinucleotide in Poly(ADP-ribose) Polymerases and ADP-Ribosylating Toxins: Implications for Structure-Based Drug Design" in Journal of Medicinal Chemistry, 53, no. 10 (2010):4038-4049,
https://doi.org/10.1021/jm1001106 . .