2x2c: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(6 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2x2c.png|left|200px]]


<!--
==acetyl-CypA:cyclosporine complex==
The line below this paragraph, containing "STRUCTURE_2x2c", creates the "Structure Box" on the page.
<StructureSection load='2x2c' size='340' side='right'caption='[[2x2c]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2x2c]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2C FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</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;'>[[1bck|1bck]], [[1c5f|1c5f]], [[1csa|1csa]], [[1cwa|1cwa]], [[1cwb|1cwb]], [[1cwc|1cwc]], [[1cwf|1cwf]], [[1cwh|1cwh]], [[1cwi|1cwi]], [[1cwj|1cwj]], [[1cwk|1cwk]], [[1cwl|1cwl]], [[1cwm|1cwm]], [[1cwo|1cwo]], [[1cya|1cya]], [[1cyb|1cyb]], [[1cyn|1cyn]], [[1ikf|1ikf]], [[1m63|1m63]], [[1mf8|1mf8]], [[1mik|1mik]], [[1qng|1qng]], [[1qnh|1qnh]], [[1xq7|1xq7]], [[2esl|2esl]], [[2oju|2oju]], [[2poy|2poy]], [[2rma|2rma]], [[2rmb|2rmb]], [[2rmc|2rmc]], [[2wfj|2wfj]], [[2x7k|2x7k]], [[2z6w|2z6w]], [[3bo7|3bo7]], [[3cys|3cys]], [[3eov|3eov]], [[1vbs|1vbs]], [[1oca|1oca]], [[2cyh|2cyh]], [[1vbt|1vbt]], [[1m9e|1m9e]], [[1rmh|1rmh]], [[1m9c|1m9c]], [[1m9y|1m9y]], [[1m9f|1m9f]], [[4cyh|4cyh]], [[1w8v|1w8v]], [[1awr|1awr]], [[1nmk|1nmk]], [[1awv|1awv]], [[1m9d|1m9d]], [[2x2a|2x2a]], [[1awt|1awt]], [[2cpl|2cpl]], [[1fgl|1fgl]], [[1m9x|1m9x]], [[5cyh|5cyh]], [[2x2d|2x2d]], [[1ak4|1ak4]], [[2alf|2alf]], [[1aws|1aws]], [[2x25|2x25]], [[1w8l|1w8l]], [[1awu|1awu]], [[1w8m|1w8m]]</div></td></tr>
{{STRUCTURE_2x2c|  PDB=2x2c  |  SCENE=  }}
<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=2x2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2c OCA], [https://pdbe.org/2x2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x2c RCSB], [https://www.ebi.ac.uk/pdbsum/2x2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x2c 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/x2/2x2c_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=2x2c 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.


===ACETYL-CYPA:CYCLOSPORINE COMPLEX===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2x2c" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20364129}}, adds the Publication Abstract to the page
*[[Cyclophilin|Cyclophilin]]
(as it appears on PubMed at http://www.pubmed.gov), where 20364129 is the PubMed ID number.
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-->
== References ==
{{ABSTRACT_PUBMED_20364129}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
[[2x2c]] is a 10 chain structure 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=2X2C OCA].
[[Category: Human]]
 
[[Category: Large Structures]]
==Reference==
<ref group="xtra">PMID:020364129</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[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: Cyclophilin-cyclosporin complex]]
[[Category: Cyclophilin-cyclosporin complex]]
[[Category: Cyclosporin some]]
[[Category: Cyclosporin some]]

Latest revision as of 11:35, 10 November 2021

acetyl-CypA:cyclosporine complexacetyl-CypA:cyclosporine complex

Structural highlights

2x2c is a 10 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:, , , , , ,
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Lammers M, Neumann H, Chin JW, James LC. Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization. Nat Chem Biol. 2010 May;6(5):331-7. Epub 2010 Apr 4. PMID:20364129 doi:10.1038/nchembio.342

2x2c, resolution 2.41Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2x2c&oldid=3476596"