2x2a

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[[Image:2x2a.png|left|200px]]
 
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==Free acetyl-CypA trigonal form==
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The line below this paragraph, containing "STRUCTURE_2x2a", creates the "Structure Box" on the page.
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<StructureSection load='2x2a' size='340' side='right'caption='[[2x2a]], [[Resolution|resolution]] 1.40&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'>[[2x2a]] 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=2X2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2A FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
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{{STRUCTURE_2x2a| PDB=2x2a | SCENE= }}
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vbs|1vbs]], [[1oca|1oca]], [[1mf8|1mf8]], [[2cyh|2cyh]], [[1cwb|1cwb]], [[1vbt|1vbt]], [[1m9e|1m9e]], [[1cwl|1cwl]], [[1cwc|1cwc]], [[1cwo|1cwo]], [[1cwi|1cwi]], [[1rmh|1rmh]], [[1cwj|1cwj]], [[2rmb|2rmb]], [[1m9c|1m9c]], [[1cwa|1cwa]], [[1cwf|1cwf]], [[3cyh|3cyh]], [[1m9y|1m9y]], [[4cyh|4cyh]], [[1m9f|1m9f]], [[1cwh|1cwh]], [[1bck|1bck]], [[1w8v|1w8v]], [[1awr|1awr]], [[1nmk|1nmk]], [[1mik|1mik]], [[1awv|1awv]], [[1m9d|1m9d]], [[1awt|1awt]], [[1fgl|1fgl]], [[2cpl|2cpl]], [[1m9x|1m9x]], [[1cwk|1cwk]], [[1m63|1m63]], [[5cyh|5cyh]], [[1ak4|1ak4]], [[3cys|3cys]], [[1w8l|1w8l]], [[2alf|2alf]], [[1aws|1aws]], [[2x25|2x25]], [[1w8m|1w8m]], [[1awu|1awu]], [[2rma|2rma]], [[1cwm|1cwm]], [[1awq|1awq]], [[2x2d|2x2d]], [[2x2c|2x2c]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=2x2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2a OCA], [https://pdbe.org/2x2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x2a RCSB], [https://www.ebi.ac.uk/pdbsum/2x2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x2a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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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/x2/2x2a_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=2x2a 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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Cyclophilin A (CypA) is a ubiquitous cis-trans prolyl isomerase with key roles in immunity and viral infection. CypA suppresses T-cell activation through cyclosporine complexation and is required for effective HIV-1 replication in host cells. We show that CypA is acetylated in diverse human cell lines and use a synthetically evolved acetyllysyl-tRNA synthetase/tRNA(CUA) pair to produce recombinant acetylated CypA in Escherichia coli. We determined atomic-resolution structures of acetylated CypA and its complexes with cyclosporine and HIV-1 capsid. Acetylation markedly inhibited CypA catalysis of cis to trans isomerization and stabilized cis rather than trans forms of the HIV-1 capsid. Furthermore, CypA acetylation antagonized the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition. Our results reveal that acetylation regulates key functions of CypA in immunity and viral infection and provide a general set of mechanisms by which acetylation modulates interactions to regulate cell function.
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===FREE ACETYL-CYPA TRIGONAL FORM===
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Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization.,Lammers M, Neumann H, Chin JW, James LC Nat Chem Biol. 2010 May;6(5):331-7. Epub 2010 Apr 4. PMID:20364129<ref>PMID:20364129</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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The line below this paragraph, {{ABSTRACT_PUBMED_20364129}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2x2a" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20364129 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20364129}}
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==About this Structure==
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[[2x2a]] is a 2 chain structure of [[Cyclophilin]] 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=2X2A OCA].
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==See Also==
==See Also==
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*[[Cyclophilin]]
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:020364129</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
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[[Category: Chin, J W.]]
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[[Category: Chin, J W]]
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[[Category: James, L C.]]
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[[Category: James, L C]]
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[[Category: Lammers, M.]]
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[[Category: Lammers, M]]
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[[Category: Neumann, H.]]
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[[Category: Neumann, H]]
[[Category: Hiv-1]]
[[Category: Hiv-1]]
[[Category: Host-virus interaction]]
[[Category: Host-virus interaction]]
[[Category: Isomerase]]
[[Category: Isomerase]]

Current revision

Free acetyl-CypA trigonal form

PDB ID 2x2a

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