NudT16
From Proteopedia
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NudT16 is a dimer | NudT16 is a dimer | ||
<Structure load='6B09' size='350' frame='true' align='right' caption='Crystal structure of HsNUDT16 in complex with diADPR (soaked)' scene='Crystal' /> | <Structure load='6B09' size='350' frame='true' align='right' caption='Crystal structure of HsNUDT16 in complex with diADPR (soaked)' scene='Crystal' /> | ||
| - | <Structure load='5VY2' size=' | + | <Structure load='5VY2' size='300' frame='true' align='right' caption='5VY2 F36A mutant' scene='Insert optional scene name here' /> |
| - | <Structure load='5JWI' size=' | + | <Structure load='5JWI' size='300' frame='true' align='right' caption='5JWI Crystal structure of Porphyromonas endodontalis DPP11 in complex with dipeptide Arg-Glu' scene='Insert optional scene name here' /> |
== Function == | == Function == | ||
Revision as of 19:27, 30 June 2020
Contents |
Introduction
NudT16 is a hydrolase and belongs to the nucleoside diphosphate-linked moiety X (Nudix) family. This protein regulates levels of 53BP1 which is a protein that recruits other proteins to the site of a DNA breakage. NudT16 has also shown in vitro to remove ADP-ribosylation through its hydrolase activities.
Structure
NudT16 is a dimer
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Function
Disease
Relevance
Structural highlights
</StructureSection>
References
Proteopedia Page Contributors and Editors (what is this?)
Hannah Campbell, Tihitina Y Aytenfisu, Michal Harel, Sandra B. Gabelli
