Prolyl hydroxylase domain: Difference between revisions
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**[[6st3]] - hPHD2 catalytic domain + Mn + pyrimidin derivative<br /> | **[[6st3]] - hPHD2 catalytic domain + Mn + pyrimidin derivative<br /> | ||
**[[6yvt]] - hPHD2 catalytic domain + Mn + pyridin derivative<br /> | **[[6yvt]] - hPHD2 catalytic domain + Mn + pyridin derivative<br /> | ||
**[[6qgv]], [[5a3u]] - hPHD2 catalytic domain + Mn + inhibitor<br /> | **[[6qgv]], [[5a3u]], [[6st3]], [[6yvt]], [[6zbn]], [[6zbo]] - hPHD2 catalytic domain + Mn + inhibitor<br /> | ||
**[[5ox6]], [[6ox5]] - hPHD2 catalytic domain + Mn + drug<br /> | **[[5ox6]], [[6ox5]] - hPHD2 catalytic domain + Mn + drug<br /> | ||
**[[5lat]], [[5lb6]], [[5lbb]], [[5lbc]], [[5lbe]], [[5lbf]], [[4uwd]] - hPHD2 catalytic domain (mutant) + Mn + quinolin derivative<br /> | **[[5lat]], [[5lb6]], [[5lbb]], [[5lbc]], [[5lbe]], [[5lbf]], [[4uwd]] - hPHD2 catalytic domain (mutant) + Mn + quinolin derivative<br /> | ||
**[[ | **[[6yvx]], [[6yvz]] - hPHD2 catalytic domain + Mn + peptide<br /> | ||
**[[6yw3]] - hPHD2 catalytic domain + Mn + peptide + oxalylglycine<br /> | |||
**[[6yw1]], [[6yw2]], [[6yw4]] - hPHD2 catalytic domain (mutant) + Mn + peptide + oxalylglycine<br /> | |||
*Prolyl hydroxylase domain containing other metal ions | *Prolyl hydroxylase domain containing other metal ions | ||
**[[2y33]] – hPHD2 catalytic domain residues | **[[2y33]] – hPHD2 catalytic domain residues + Zn + quinolin derivative – human<br /> | ||
**[[3ouh]], [[3oui]], [[5v18]] - hPHD2 catalytic domain + Fe + inhibitor<br /> | **[[3ouh]], [[3oui]], [[5v18]], [[6nmq]], [[6yvw]], [[6yw0]] - hPHD2 catalytic domain + Fe + inhibitor<br /> | ||
**[[4kbz]] - hPHD2 catalytic domain (mutant) + Fe + inhibitor<br /> | **[[4kbz]] - hPHD2 catalytic domain (mutant) + Fe + inhibitor<br /> | ||
**[[4jzr]] - hPHD2 catalytic domain + Ni + inhibitor<br /> | **[[4jzr]] - hPHD2 catalytic domain + Ni + inhibitor<br /> | ||
Revision as of 14:00, 1 February 2022
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.
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3D Structures of prolyl hydroxylase domain3D Structures of prolyl hydroxylase domain
Updated on 01-February-2022
ReferencesReferences
- ↑ Stolze IP, Mole DR, Ratcliffe PJ. Regulation of HIF: prolyl hydroxylases. Novartis Found Symp. 2006;272:15-25; discussion 25-36. PMID:16686427
- ↑ 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.
Created with the participation of Andrew Winslow.