Journal of Biological Chemistry
Protein Structure and FoldingStructure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition
Cited by (0)
The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
This article contains Figs. S1–S6 and Table S1.
The atomic coordinates and structure factors (codes 6D36 and 6D3A) have been deposited in the Protein Data Bank (http://wwpdb.org/).
- 1
Both authors contributed equally to this work.
- 2
Supported by the Intramural Research Program, NHLBI, National Institutes of Health.
- 4
The abbreviations used are:
- PARylation
poly(ADP-ribosyl)ation
- ARH
ADP-ribosyl-acceptor hydrolase
- PAR
poly(ADP-ribose)
- PARP
PAR polymerase
- PARG
PAR glycohydrolase
- PTM
post-translational modification
- MAR
mono(ADP-ribose)
- ADPR
ADP-ribose
- AIF
apoptosis-inducing factor
- MARylation
mono(ADP-ribosyl)ation
- FL
full-length
- r.m.s.d.
root mean square deviation
- ADP-HPD
adenosine diphosphate (hydroxymethyl)pyrrolidine-2′,3′-diol.