1mze: Difference between revisions

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-[[Image:1mze.png|left|200px]]
-{{STRUCTURE_1mze|  PDB=1mze  |  SCENE=  }}
+==Human Factor Inhibiting HIF (FIH1)==
+<StructureSection load='1mze' size='340' side='right'caption='[[1mze]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-===Human Factor Inhibiting HIF (FIH1)===
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1mze]] 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=1MZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZE FirstGlance]. <br>
-{{ABSTRACT_PUBMED_12432100}}
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
-==About this Structure==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mze OCA], [https://pdbe.org/1mze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mze RCSB], [https://www.ebi.ac.uk/pdbsum/1mze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mze ProSAT]</span></td></tr>
-[[1mze]] is a 1 chain structure of [[Factor inhibiting HIF]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZE OCA].
+</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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mze_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mze ConSurf].
+<div style="clear:both"></div>
 ==See Also==
 *[[Factor inhibiting HIF|Factor inhibiting HIF]]
+*[[Hypoxia-Inducible factor 1 alpha inhibitor|Hypoxia-Inducible factor 1 alpha inhibitor]]
-==Reference==
+== References ==
-<ref group="xtra">PMID:012432100</ref><references group="xtra"/>
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bruick, R K.]]
+[[Category: Large Structures]]
-[[Category: Deisenhofer, J.]]
+[[Category: Bruick RK]]
-[[Category: III, C E.Dann.]]
+[[Category: Dann III CE]]
-[[Category: Beta-jellyroll]]
+[[Category: Deisenhofer J]]
-[[Category: Oxidoreductase]]