2x2d
From Proteopedia
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| - | [[Image:2x2d.png|left|200px]] | ||
| - | + | ==acetyl-CypA:HIV-1 N-term capsid domain complex== | |
| + | <StructureSection load='2x2d' size='340' side='right'caption='[[2x2d]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2x2d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2D FirstGlance]. <br> | ||
| + | </td></tr><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> | ||
| + | <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]], [[1cwl|1cwl]], [[1m9e|1m9e]], [[1cwc|1cwc]], [[1cwi|1cwi]], [[1cwo|1cwo]], [[1rmh|1rmh]], [[1cwj|1cwj]], [[2rmb|2rmb]], [[1m9c|1m9c]], [[1cwa|1cwa]], [[1cwf|1cwf]], [[1m9y|1m9y]], [[3cyh|3cyh]], [[4cyh|4cyh]], [[1m9f|1m9f]], [[1cwh|1cwh]], [[1bck|1bck]], [[1w8v|1w8v]], [[1awr|1awr]], [[1nmk|1nmk]], [[1mik|1mik]], [[1awv|1awv]], [[1m9d|1m9d]], [[2cpl|2cpl]], [[2x2a|2x2a]], [[1fgl|1fgl]], [[1awt|1awt]], [[1m9x|1m9x]], [[1m63|1m63]], [[1cwk|1cwk]], [[5cyh|5cyh]], [[1ak4|1ak4]], [[1w8l|1w8l]], [[1aws|1aws]], [[3cys|3cys]], [[2alf|2alf]], [[2x25|2x25]], [[1awu|1awu]], [[1w8m|1w8m]], [[2c55|2c55]], [[1cwm|1cwm]], [[2rma|2rma]], [[1awq|1awq]], [[2x2c|2x2c]]</div></td></tr> | ||
| + | <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2d OCA], [https://pdbe.org/2x2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x2d RCSB], [https://www.ebi.ac.uk/pdbsum/2x2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x2d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x2/2x2d_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2x2d ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2x2d" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Cyclophilin|Cyclophilin]] | + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] |
| - | *[[Gag polyprotein|Gag polyprotein]] | + | *[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]] |
| - | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |
| - | == | + | == References == |
| - | < | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | [[Category: Chin, J W | + | [[Category: Chin, J W]] |
| - | [[Category: James, L C | + | [[Category: James, L C]] |
| - | [[Category: Lammers, M | + | [[Category: Lammers, M]] |
| - | [[Category: Neumann, H | + | [[Category: Neumann, H]] |
[[Category: Host-virus interaction]] | [[Category: Host-virus interaction]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
Current revision
acetyl-CypA:HIV-1 N-term capsid domain complex
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