4nr1: Difference between revisions

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-'''Unreleased structure'''
-The entry 4nr1 is ON HOLD  until Paper Publication
+==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==
+<StructureSection load='4nr1' size='340' side='right'caption='[[4nr1]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4nr1]] is a 2 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [https://pdbe.org/4nr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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>
-Authors: Scotti, J.S., McDonough, M.A., Schofield, C.J.
+==See Also==
+*[[Factor inhibiting HIF|Factor inhibiting HIF]]
-Description: Structure of an oxygenase in complex with substrate
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Mcdonough, M.A]]
+__TOC__
-[[Category: Scotti, J.S]]
+</StructureSection>
-[[Category: Schofield, C.J]]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: McDonough MA]]
+[[Category: Schofield CJ]]
+[[Category: Scotti JS]]