2x2d: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2x2d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X2D FirstGlance]. <br> | <table><tr><td colspan='2'>[[2x2d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X2D FirstGlance]. <br> | ||
</td></tr><tr><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> | </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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x2d RCSB], [http://www.ebi.ac.uk/pdbsum/2x2d PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x2d RCSB], [http://www.ebi.ac.uk/pdbsum/2x2d PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 37: | Line 39: | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[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]] | ||
Revision as of 00:45, 25 December 2014
ACETYL-CYPA:HIV-1 N-TERM CAPSID DOMAIN COMPLEXACETYL-CYPA:HIV-1 N-TERM CAPSID DOMAIN COMPLEX
Structural highlights
Function[PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCyclophilin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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