Prolyl hydroxylase domain: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
New page: {{STRUCTURE_3hqu| PDB=3hqu | SIZE=400| SCENE= |right|CAPTION=PHD2 with Fe+2 complex with HIF 1 α C terminal and iodoisoquinolin inhibitor, 3hqu }} '''Prolyl hydroxylase domain''...
 
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
{{STRUCTURE_3hqu|  PDB=3hqu  | SIZE=400| SCENE= |right|CAPTION=PHD2 with Fe+2 complex with HIF 1 α C terminal and iodoisoquinolin inhibitor, [[3hqu]] }}   
{{STRUCTURE_3hqu|  PDB=3hqu  | SIZE=400| SCENE= |right|CAPTION=PHD2 with Fe+2 complex with HIF 1 α C terminal and iodoisoquinolin inhibitor, [[3hqu]] }}   
   
   
'''Prolyl hydroxylase domain''' (PHD) proteins mediate oxygen-dependent degradation of Hypoxia-inducible factor (HIF) α subunit.  They include PHD1, PHD2 and PHD3.  The PHD is a Fe+2/oxogluterate (2OG)-dependent enzyme.
'''Prolyl hydroxylase domain''' (PHD) proteins mediate oxygen-dependent degradation of Hypoxia-inducible factor (HIF) α subunit.  They include PHD1, PHD2 and PHD3.  The PHD is a Fe+2/oxogluterate (2OG)-dependent enzyme.  For more detalis see [[Molecular Playground/ Prolyl Hydroxylase Domain (PHD) Enzyme]].


{{TOC limit|limit=2}}
{{TOC limit|limit=2}}

Revision as of 12:22, 27 July 2011

Template:STRUCTURE 3hqu

Prolyl hydroxylase domain (PHD) proteins mediate oxygen-dependent degradation of Hypoxia-inducible factor (HIF) α subunit. They include PHD1, PHD2 and PHD3. The PHD is a Fe+2/oxogluterate (2OG)-dependent enzyme. For more detalis see Molecular Playground/ Prolyl Hydroxylase Domain (PHD) Enzyme.

3D Structures of prolyl hydroxylase domain3D Structures of prolyl hydroxylase domain

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

Michal Harel, Alexander Berchansky, Joel L. Sussman