Prolyl hydroxylase domain: Difference between revisions

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Michal Harel, Alexander Berchansky, Joel L. Sussman

Revision as of 16:41, 13 June 2012 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary ← Older edit		Revision as of 15:02, 12 November 2012 view source Michal Harel (talk \| contribs) 31,761 edits No edit summary Newer edit →
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	{{STRUCTURE_3ouh\| PDB=3ouh \| SIZE=400\| SCENE= \|right\|CAPTION=Human PHD2 catalytic domain + Fe + inhibitor, [[3ouh]] }}		{{STRUCTURE_3ouh\| PDB=3ouh \| SIZE=400\| SCENE= \|right\|CAPTION=Human PHD2 catalytic domain complex with Fe+2 ion, inhibitor and sulfate, [[3ouh]] }}

	'''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. [[3ouh]] is the crystallized structure of the enzyme PHD2, an [[oxidoreductase]] that is 237 amino acids long with a molecular weight of 27 kDa. [[3ouh]] is found in [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and is a homolog of [http://en.wikipedia.org/wiki/EGLN1 EGLN1] found in [http://en.wikipedia.org/wiki/Caenorhabditis_elegans C. elegans].		'''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. [[3ouh]] is the crystallized structure of the enzyme PHD2, an [[oxidoreductase]] that is 237 amino acids long with a molecular weight of 27 kDa. [[3ouh]] is found in [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and is a homolog of [http://en.wikipedia.org/wiki/EGLN1 EGLN1] found in [http://en.wikipedia.org/wiki/Caenorhabditis_elegans C. elegans].