1l3e

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[[Image:1l3e.gif|left|200px]]
 
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==NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex==
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The line below this paragraph, containing "STRUCTURE_1l3e", creates the "Structure Box" on the page.
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<StructureSection load='1l3e' size='340' side='right'caption='[[1l3e]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1l3e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L3E FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1l3e| PDB=1l3e | SCENE= }}
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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=1l3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3e OCA], [https://pdbe.org/1l3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l3e RCSB], [https://www.ebi.ac.uk/pdbsum/1l3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l3e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref> <ref>PMID:11566883</ref> <ref>PMID:11292861</ref> <ref>PMID:15465032</ref> <ref>PMID:16543236</ref> <ref>PMID:16973622</ref> <ref>PMID:17610843</ref> <ref>PMID:19528298</ref> <ref>PMID:20624928</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/1l3e_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1l3e ConSurf].
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<div style="clear:both"></div>
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'''NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex'''
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==See Also==
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*[[Factor inhibiting HIF|Factor inhibiting HIF]]
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*[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]]
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==Overview==
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== References ==
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Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators. We report the solution structure of the cysteine/histidine-rich 1 (CH1) domain of p300 bound to the C-terminal transactivation domain of HIF-1 alpha. CH1 has a triangular geometry composed of four alpha-helices with three intervening Zn(2+)-coordinating centers. CH1 serves as a scaffold for folding of the HIF-1 alpha C-terminal transactivation domain, which forms a vise-like clamp on the CH1 domain that is stabilized by extensive hydrophobic and polar interactions. The structure reveals the mechanism of specific recognition of p300 by HIF-1 alpha, and shows how HIF-1 alpha transactivation is regulated by asparagine hydroxylation.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1L3E is a [[Protein complex]] structure of sequences 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=1L3E OCA].
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==Reference==
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Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha., Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ, Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11959990 11959990]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Eck, M J.]]
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[[Category: Eck MJ]]
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[[Category: Freedman, S J.]]
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[[Category: Freedman SJ]]
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[[Category: Kung, A L.]]
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[[Category: Kung AL]]
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[[Category: Livingston, D M.]]
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[[Category: Livingston DM]]
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[[Category: Poy, F.]]
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[[Category: Poy F]]
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[[Category: Sun, Z J.]]
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[[Category: Sun ZJ]]
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[[Category: Wagner, G.]]
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[[Category: Wagner G]]
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[[Category: Protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:29:40 2008''
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Current revision

NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex

PDB ID 1l3e

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