1lqb

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{{Seed}}
 
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[[Image:1lqb.png|left|200px]]
 
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==Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex==
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The line below this paragraph, containing "STRUCTURE_1lqb", creates the "Structure Box" on the page.
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<StructureSection load='1lqb' size='340' side='right'caption='[[1lqb]], [[Resolution|resolution]] 2.00&Aring;' 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'>[[1lqb]] is a 4 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=1LQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQB 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">X-ray diffraction, [[Resolution|Resolution]] 2&#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=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1lqb| PDB=1lqb | 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=1lqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqb OCA], [https://pdbe.org/1lqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqb RCSB], [https://www.ebi.ac.uk/pdbsum/1lqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ELOC_HUMAN ELOC_HUMAN] SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).<ref>PMID:15590694</ref> The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.<ref>PMID:15590694</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/lq/1lqb_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=1lqb 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 factor-1 (HIF-1) is a transcriptional complex that controls cellular and systemic homeostatic responses to oxygen availability. HIF-1 alpha is the oxygen-regulated subunit of HIF-1, an alpha beta heterodimeric complex. HIF-1 alpha is stable in hypoxia, but in the presence of oxygen it is targeted for proteasomal degradation by the ubiquitination complex pVHL, the protein of the von Hippel Lindau (VHL) tumour suppressor gene and a component of an E3 ubiquitin ligase complex. Capture of HIF-1 alpha by pVHL is regulated by hydroxylation of specific prolyl residues in two functionally independent regions of HIF-1 alpha. The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL. Optimized hydrogen bonding to the buried hydroxyprolyl group confers precise discrimination between hydroxylated and unmodified prolyl residues. This mechanism provides a new focus for development of therapeutic agents to modulate cellular responses to hypoxia.
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===Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex===
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Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.,Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY Nature. 2002 Jun 27;417(6892):975-8. Epub 2002 Jun 5. PMID:12050673<ref>PMID:12050673</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 1lqb" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12050673}}, adds the Publication Abstract to the page
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12050673 is the PubMed ID number.
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*[[Factor inhibiting HIF|Factor inhibiting HIF]]
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== References ==
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{{ABSTRACT_PUBMED_12050673}}
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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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1LQB is a 4 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=1LQB OCA].
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==Reference==
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<ref group="xtra">PMID:12050673</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Claridge, T D.]]
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[[Category: Large Structures]]
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[[Category: Harlos, K.]]
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[[Category: Claridge TD]]
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[[Category: Hon, W C.]]
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[[Category: Harlos K]]
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[[Category: Jones, E Y.]]
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[[Category: Hon WC]]
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[[Category: Maxwell, P H.]]
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[[Category: Jones EY]]
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[[Category: Pugh, C W.]]
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[[Category: Maxwell PH]]
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[[Category: Ratcliffe, P J.]]
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[[Category: Pugh CW]]
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[[Category: Schofield, C J.]]
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[[Category: Ratcliffe PJ]]
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[[Category: Stuart, D I.]]
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[[Category: Schofield CJ]]
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[[Category: Wilson, M I.]]
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[[Category: Stuart DI]]
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[[Category: Cancer]]
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[[Category: Wilson MI]]
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[[Category: Prolyl hydroxylation]]
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[[Category: Protein-peptide complex]]
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[[Category: Proteosomal degradation]]
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[[Category: Tumor suppressor]]
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[[Category: Ubiquitin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:17:59 2009''
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Current revision

Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex

PDB ID 1lqb

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