J. Biol. Chem., 2015; 290 (12)

J. Biol. Chem. has selected the picture we produced for Tobias Karlberg (Karolinska Insitute, Stockholm) to illustrate his article "Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein".1

This illustration represents the catalytic domain of PARP15 (shown as a blue glass molecular surface) overlayed with PARP13 (displayed as pink outlines). PARP13 harbours an original loop (shown in flashy red) which blocks the NAD-binding site (NAD is shown as stick-and-ball mode). Moreover, the tyrosine (colored in flashy green) which is an essential discriminant for substrate binding lacks in PARP13. These two elements explain why PARP13 lacks ADP-ribosyltransferase activity.

Here is a link to the full text version of the article.

1.  Karlberg T, Klepsch M, Thorsell AG, Andersson CD, Linusson A, Schüler H. Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein. Journal of Biological Chemistry. 2015 Mar 20;290(12):7336-44.