Sandbox Reserved 1452: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Maaz Majid (talk | contribs) No edit summary |
Maaz Majid (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
{{Sandbox_Reserved_Telford2018}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <scene name='77/778332/1vax/1'>Text To Be Displayed</scene>{{Sandbox_Reserved_Telford2018}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Uricase== | ==Uricase== | ||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| Line 24: | Line 24: | ||
== Structural highlights == | == Structural highlights == | ||
Uricase is mainly located in the liver where it forms an elctron dense crystalline core in peroxisomes. It is a tetramer of identical subunits each containing copper binding sites. X-ray crystallography shows that uric acid binds to the active site as a monoanion and is deprotonated as a dianion which is then stabilized by Arg 176 and Gln 228. Uricase can be inhibited by both cyanide and chloride ions. Oxonate competitively inhibits uricase. | Uricase is mainly located in the liver where it forms an elctron dense crystalline core in peroxisomes. It is a tetramer of identical subunits each containing copper binding sites. X-ray crystallography shows that uric acid binds to the active site as a monoanion and is deprotonated as a dianion which is then stabilized by <scene name='77/778332/1vax/1'>Arg 176</scene> and Gln 228. Uricase can be inhibited by both cyanide and chloride ions. Oxonate competitively inhibits uricase. | ||
This is <scene name='77/778332/1vax/1'>uricase</scene> without a ligand. | This is <scene name='77/778332/1vax/1'>uricase</scene> without a ligand. | ||
You can view uricase with a ligand <scene name='77/778332/4mb8/1'>here.</scene> | You can view uricase with a ligand <scene name='77/778332/4mb8/1'>here.</scene> | ||