5v1b

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'''Unreleased structure'''
 
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The entry 5v1b is ON HOLD until Paper Publication
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==Structure of PHD1 in complex with 1,2,4-Triazolo-[1,5-a]pyridine==
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<StructureSection load='5v1b' size='340' side='right'caption='[[5v1b]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5v1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V1B FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8UY:4-([1,2,4]triazolo[1,5-a]pyridin-5-yl)benzonitrile'>8UY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1b OCA], [https://pdbe.org/5v1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v1b RCSB], [https://www.ebi.ac.uk/pdbsum/5v1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EGLN2_HUMAN EGLN2_HUMAN] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferentially recognized via a LXXLAP motif.<ref>PMID:11595184</ref> <ref>PMID:12181324</ref> <ref>PMID:16509823</ref> <ref>PMID:17114296</ref> <ref>PMID:19339211</ref> <ref>PMID:23932902</ref>
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Authors: Skene, R.J.
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==See Also==
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*[[Polyl hydroxylase domain 3D structures|Polyl hydroxylase domain 3D structures]]
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Description: Structure of PHD1 in complex with 1,2,4-Triazolo-[1,5-a]pyridine
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Skene, R.J]]
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Skene RJ]]

Current revision

Structure of PHD1 in complex with 1,2,4-Triazolo-[1,5-a]pyridine

PDB ID 5v1b

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