Prolyl hydroxylase domain: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='400' side='right' scene='45/459221/Cv/1' caption='Human PHD2 catalytic domain complex with Fe+2 ion (orange), inhibitor and sulfate, [[3ouh]]' pspeed='8'> | ||
'''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]. | See also [[Hydroxylase]] | ||
The protein has three ligands: <scene name='45/459221/Cv/ | |||
'''Prolyl hydroxylase domain''' (PHD) or '''egl nine homolog 1''' (PHD2/EGLN1) 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]. | |||
The protein has three ligands: <scene name='45/459221/Cv/4'>O14</scene> (a 1-(5-chloro-6-fluoro-1H-benzimidazol-2-yl)-1H-pyrazole-4-carboxylic acid), <scene name='45/459221/Cv/3'>Fe+2 (an iron ion)</scene>, and SO<sub>4</sub> (a sulfate ion). Water molecules are shown as red spheres. It is involved in mediating physiological responses to [http://en.wikipedia.org/wiki/Hypoxia_(medical) hypoxia] by degrading the transcription factor of a hypoxia-inducible factor HIF1-α. In hypoxic conditions, the activity of PHD2 lessens, causing an increase in HIF1-α, resulting in secretion of erythropoietin, anaerobic [[glycolysis]], and angiogenesis<ref>PMID:16686427</ref>. | |||
<ref>Rosen M D, Venkatesan H, Peltier H M, Bembenek S D, Kanelakis K C, Zhao L X, Leonard B E, Hocutt F M, Wu X, Palomino H L, Brondtetter T I, Haugh P V, Cagnon L, Yan W, Liotta L A, Young A, Mirzadegan T, Shankley N P, Barrett T D, Rabinowitz M H. Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues. ACS Medicinal Chemical Letters. 2010 Oct 5.</ref> For more detalis see [[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]. | <ref>Rosen M D, Venkatesan H, Peltier H M, Bembenek S D, Kanelakis K C, Zhao L X, Leonard B E, Hocutt F M, Wu X, Palomino H L, Brondtetter T I, Haugh P V, Cagnon L, Yan W, Liotta L A, Young A, Mirzadegan T, Shankley N P, Barrett T D, Rabinowitz M H. Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues. ACS Medicinal Chemical Letters. 2010 Oct 5.</ref> For more detalis see [[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]. | ||
== 3D Structures of prolyl hydroxylase domain == | == 3D Structures of prolyl hydroxylase domain == | ||
[[ | [[Polyl hydroxylase domain 3D structures]] | ||
==References== | ==References== | ||
<references/> | <references/> | ||
</StructureSection> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
<br /> | <br /> | ||
Created with the participation of [[User:Andrew Winslow|Andrew Winslow]]. | Created with the participation of [[User:Andrew Winslow|Andrew Winslow]]. | ||
Latest revision as of 10:33, 13 September 2023
See also Hydroxylase Prolyl hydroxylase domain (PHD) or egl nine homolog 1 (PHD2/EGLN1) 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 Homo sapiens and is a homolog of EGLN1 found in C. elegans. The protein has three ligands: (a 1-(5-chloro-6-fluoro-1H-benzimidazol-2-yl)-1H-pyrazole-4-carboxylic acid), , and SO4 (a sulfate ion). Water molecules are shown as red spheres. It is involved in mediating physiological responses to hypoxia by degrading the transcription factor of a hypoxia-inducible factor HIF1-α. In hypoxic conditions, the activity of PHD2 lessens, causing an increase in HIF1-α, resulting in secretion of erythropoietin, anaerobic glycolysis, and angiogenesis[1]. [2] For more detalis see Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme. 3D Structures of prolyl hydroxylase domainPolyl hydroxylase domain 3D structures References
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Created with the participation of Andrew Winslow.