NudT16: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 8: Line 8:
<Structure load='6W6Z' size='350' frame='true' align='right' caption='6W6Z' scene='Insert optional scene name here' />
<Structure load='6W6Z' size='350' frame='true' align='right' caption='6W6Z' scene='Insert optional scene name here' />
<Structure load='5VY2' size='350' frame='true' align='right' caption='5VY2 F36A mutant' scene='Insert optional scene name here' />
<Structure load='5VY2' size='350' frame='true' align='right' caption='5VY2 F36A mutant' scene='Insert optional scene name here' />
<Structure load='5JWI' size='350' frame='true' align='right' caption='5JWI' scene='Insert optional scene name here' />
<Structure load='5JWI' size='350' 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 22:09, 30 June 2020

IntroductionIntroduction

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.

StructureStructure

NudT16

NudT16 is a dimer

Crystal structure of HsNUDT16 in complex with diADPR (soaked)

Drag the structure with the mouse to rotate

6W6Z

Drag the structure with the mouse to rotate

5VY2 F36A mutant

Drag the structure with the mouse to rotate

5JWI Crystal structure of Porphyromonas endodontalis DPP11 in complex with dipeptide Arg-Glu

Drag the structure with the mouse to rotate

FunctionFunction

DiseaseDisease

RelevanceRelevance

Structural highlightsStructural highlights

</StructureSection>

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Tihitina Y Aytenfisu, Hannah Campbell, Sandra B. Gabelli, Michal Harel