Sandbox Reserved 1098: Difference between revisions

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The protein <scene name='82/829351/Parg/1'>PARG</scene> folds into an ADP-ribose-binding macro domain with an N-terminal extension. It also consists of a diphosphate-binding loop on one side of an ADP-ribose binding cavity. On the other side there are several amino acids matching to the specific PARG signature sequence.  
The protein <scene name='82/829351/Parg/1'>PARG</scene> folds into an ADP-ribose-binding macro domain with an N-terminal extension. It also consists of a diphosphate-binding loop on one side of an ADP-ribose binding cavity. On the other side there are several amino acids matching to the specific PARG signature sequence.  
In the macro domain fold, a loop is inserted to welcome the Glu115 side chain protecting the active site of the PARG protein. This loop gives PARG the ability to hydrolyze PAR. The  <scene name='82/829351/Parg_active_site/1'>hydrolysis of PAR happens in PARG catalytic domain</scene>. (PAR is represented here in pink).
In the macro domain fold, a loop is inserted to welcome the Glu115 side chain protecting the active site of the PARG protein. This loop gives PARG the ability to hydrolyze PAR. The  <scene name='82/829351/Parg_active_site/1'>hydrolysis of PAR happens in PARG catalytic domain</scene>. (PAR is represented here in pink).
Concerning the ligand pairing with the PARG protein only a small difference can be observed for the amino acids Val226 and Phe227 <ref>PMID: 21892188</ref>.
 


=== Quaternary Structure ===
=== Quaternary Structure ===