6h9j
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (229-255)== | |
| - | + | <StructureSection load='6h9j' size='340' side='right'caption='[[6h9j]], [[Resolution|resolution]] 1.83Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6h9j]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H9J FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9j OCA], [http://pdbe.org/6h9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h9j RCSB], [http://www.ebi.ac.uk/pdbsum/6h9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9j ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/TRPV3_HUMAN TRPV3_HUMAN]] Mutilating palmoplantar keratoderma with periorificial keratotic plaques. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref> [[http://www.uniprot.org/uniprot/TRPV3_HUMAN TRPV3_HUMAN]] Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen).<ref>PMID:12077604</ref> <ref>PMID:12077606</ref> <ref>PMID:21593771</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Clifton, I J]] | ||
| + | [[Category: Hopkinson, R J]] | ||
| + | [[Category: Leissing, T M]] | ||
| + | [[Category: Lu, X]] | ||
| + | [[Category: Saward, B G]] | ||
| + | [[Category: Schofield, C J]] | ||
| + | [[Category: Activator-inhibitor]] | ||
| + | [[Category: Ard]] | ||
| + | [[Category: Asparaginyl/aspartyl hydroxylase]] | ||
| + | [[Category: Beta-hydroxylation]] | ||
| + | [[Category: Channel]] | ||
| + | [[Category: Dioxygenase]] | ||
| + | [[Category: Dsbh]] | ||
| + | [[Category: Facial triad]] | ||
| + | [[Category: Gene regulation]] | ||
| + | [[Category: Ion channel]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Non-heme]] | ||
| + | [[Category: Oxidoreductase ankyrin]] | ||
| + | [[Category: Oxidoreductase-peptide complex]] | ||
| + | [[Category: Oxygenase]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Signaling]] | ||
| + | [[Category: Transcription]] | ||
| + | [[Category: Trpv channel]] | ||
Current revision
Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (229-255)
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Categories: Large Structures | Clifton, I J | Hopkinson, R J | Leissing, T M | Lu, X | Saward, B G | Schofield, C J | Activator-inhibitor | Ard | Asparaginyl/aspartyl hydroxylase | Beta-hydroxylation | Channel | Dioxygenase | Dsbh | Facial triad | Gene regulation | Ion channel | Membrane protein | Metal-binding | Non-heme | Oxidoreductase ankyrin | Oxidoreductase-peptide complex | Oxygenase | Protein binding | Signaling | Transcription | Trpv channel
