3h82

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{{Seed}}
 
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[[Image:3h82.jpg|left|200px]]
 
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==Crystal structure of the high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains with the artificial ligand THS020==
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The line below this paragraph, containing "STRUCTURE_3h82", creates the "Structure Box" on the page.
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<StructureSection load='3h82' size='340' side='right'caption='[[3h82]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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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'>[[3h82]] 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=3H82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H82 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]] 1.5&#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=020:N-(FURAN-2-YLMETHYL)-2-NITRO-4-(TRIFLUOROMETHYL)ANILINE'>020</scene></td></tr>
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{{STRUCTURE_3h82| PDB=3h82 | 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=3h82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h82 OCA], [https://pdbe.org/3h82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h82 RCSB], [https://www.ebi.ac.uk/pdbsum/3h82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h82 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARNT_HUMAN ARNT_HUMAN] Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.
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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/h8/3h82_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=3h82 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hypoxia-inducible factors (HIFs) are heterodimeric transcription factors responsible for the metazoan hypoxia response and promote tumor growth, metastasis, and resistance to cancer treatment. The C-terminal Per-ARNT-Sim (PAS) domain of HIF2alpha (HIF2alpha PAS-B) contains a preformed solvent-inaccessible cavity that binds artificial ligands that allosterically perturb the formation of the HIF heterodimer. To better understand how small molecules bind within this domain, we examined the structures and equilibrium and transition-state thermodynamics of HIF2alpha PAS-B with several artificial ligands using isothermal titration calorimetry, NMR exchange spectroscopy, and X-ray crystallography. Rapid association rates reveal that ligand binding is not dependent upon a slow conformational change in the protein to permit ligand access, despite the closed conformation observed in the NMR and crystal structures. Compensating enthalpic and entropic contributions to the thermodynamic barrier for ligand binding suggest a binding-competent transition state characterized by increased structural disorder. Finally, molecular dynamics simulations reveal conversion between open and closed conformations of the protein and pathways of ligand entry into the binding pocket.
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===Crystal structure of the high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains with the artificial ligand THS020===
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Principles of ligand binding within a completely buried cavity in HIF2alpha PAS-B.,Key J, Scheuermann TH, Anderson PC, Daggett V, Gardner KH J Am Chem Soc. 2009 Dec 9;131(48):17647-54. PMID:19950993<ref>PMID:19950993</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3h82" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19950993}}, adds the Publication Abstract to the page
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*[[Factor inhibiting HIF|Factor inhibiting HIF]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19950993 is the PubMed ID number.
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*[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]]
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== References ==
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{{ABSTRACT_PUBMED_19950993}}
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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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3H82 is a 2 chains 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=3H82 OCA].
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==Reference==
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<ref group="xtra">PMID:19950993</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Anderson, P C.]]
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[[Category: Large Structures]]
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[[Category: Daggett, V.]]
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[[Category: Anderson PC]]
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[[Category: Gardner, K H.]]
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[[Category: Daggett V]]
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[[Category: Key, J M.]]
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[[Category: Gardner KH]]
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[[Category: Scheuermann, T H.]]
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[[Category: Key JM]]
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[[Category: Activator]]
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[[Category: Scheuermann TH]]
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[[Category: Alternative splicing]]
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[[Category: Angiogenesis]]
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[[Category: Congenital erythrocytosis]]
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[[Category: Developmental protein]]
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[[Category: Differentiation]]
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[[Category: Disease mutation]]
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[[Category: Dna-binding]]
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[[Category: Heterodimer]]
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[[Category: Hydroxylation]]
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[[Category: Nucleus]]
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[[Category: Pas domain]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Protein ligand complex.]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Ubl conjugation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 13:56:00 2010''
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Current revision

Crystal structure of the high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains with the artificial ligand THS020

PDB ID 3h82

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