1hv2

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{{Seed}}
 
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[[Image:1hv2.png|left|200px]]
 
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==SOLUTION STRUCTURE OF YEAST ELONGIN C IN COMPLEX WITH A VON HIPPEL-LINDAU PEPTIDE==
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The line below this paragraph, containing "STRUCTURE_1hv2", creates the "Structure Box" on the page.
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<StructureSection load='1hv2' size='340' side='right'caption='[[1hv2]]' 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'>[[1hv2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HV2 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hv2 OCA], [https://pdbe.org/1hv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hv2 RCSB], [https://www.ebi.ac.uk/pdbsum/1hv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hv2 ProSAT]</span></td></tr>
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{{STRUCTURE_1hv2| PDB=1hv2 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ELOC_YEAST ELOC_YEAST] Prevents degradation of interacting proteins like PCL6 by the proteasome.<ref>PMID:11864988</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/hv/1hv2_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=1hv2 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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Elongin is a transcription elongation factor that stimulates the rate of elongation by suppressing transient pausing by RNA polymerase II at many sites along the DNA. It is heterotrimeric in mammals, consisting of elongins A, B and C subunits, and bears overall similarity to a class of E3 ubiquitin ligases known as SCF (Skp1-Cdc53 (cullin)-F-box) complexes. A subcomplex of elongins B and C is a target for negative regulation by the von Hippel-Lindau (VHL) tumor-suppressor protein. Elongin C from Saccharomyces cerevisiae, Elc1, exhibits high sequence similarity to mammalian elongin C. Using NMR spectroscopy we have determined the three-dimensional structure of Elc1 in complex with a human VHL peptide, VHL(157-171), representing the major Elc1 binding site. The bound VHL peptide is entirely helical. Elc1 utilizes two C-terminal helices and an intervening loop to form a binding groove that fits VHL(157-171). Chemical shift perturbation and dynamics analyses reveal that a global conformational change accompanies Elc1/VHL(157-171) complex formation. Moreover, the disappearance of conformational exchange phenomena on the microsecond to millisecond time scale within Elc1 upon VHL peptide binding suggests a role for slow internal motions in ligand recognition.
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===SOLUTION STRUCTURE OF YEAST ELONGIN C IN COMPLEX WITH A VON HIPPEL-LINDAU PEPTIDE===
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Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide.,Botuyan MV, Mer G, Yi GS, Koth CM, Case DA, Edwards AM, Chazin WJ, Arrowsmith CH J Mol Biol. 2001 Sep 7;312(1):177-86. PMID:11545595<ref>PMID:11545595</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 1hv2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11545595}}, 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 11545595 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11545595}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1HV2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HV2 OCA].
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[[Category: Mus musculus]]
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==Reference==
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<ref group="xtra">PMID:11545595</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Botuyan, M V.]]
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[[Category: Botuyan MV]]
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[[Category: Case, D A.]]
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[[Category: Case DA]]
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[[Category: Chazin, W J.]]
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[[Category: Chazin WJ]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Koth, C M.]]
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[[Category: Koth CM]]
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[[Category: Mer, G.]]
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[[Category: Mer G]]
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[[Category: Yi, G S.]]
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[[Category: Yi G-S]]
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[[Category: Protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:21:28 2009''
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Current revision

SOLUTION STRUCTURE OF YEAST ELONGIN C IN COMPLEX WITH A VON HIPPEL-LINDAU PEPTIDE

PDB ID 1hv2

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