View source for 3tne


==The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir==
<StructureSection load='3tne' size='340' side='right'caption='[[3tne]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tne]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis Candida parapsilosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TNE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RIT:RITONAVIR'>RIT</scene></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=3tne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tne OCA], [https://pdbe.org/3tne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tne RCSB], [https://www.ebi.ac.uk/pdbsum/3tne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tne ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARP1_CANPA CARP1_CANPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Secreted aspartic proteases (Saps) are extracellular proteolytic enzymes that enhance the virulence of Candida pathogens. These enzymes therefore represent possible targets for therapeutic drug design. Saps are inhibited by nanomolar concentrations of the classical inhibitor of aspartic proteases pepstatin A and also by the inhibitors of the HIV protease, but with the K(i) of micromolar values or higher. To contribute to the discussion regarding whether HIV protease inhibitors can act against opportunistic mycoses by the inhibition of Saps, we determined the structure of Sapp1p from Candida parapsilosis in complex with ritonavir (RTV), a clinically used inhibitor of the HIV protease. The crystal structure refined at resolution 2.4 A proved binding of RTV into the active site of Sapp1p and provided the structural information necessary to evaluate the stability and specificity of the protein-inhibitor interaction.

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir.,Dostal J, Brynda J, Hruskova-Heidingsfeldova O, Pachl P, Pichova I, Rezacova P J Enzyme Inhib Med Chem. 2012 Feb;27(1):160-5. Epub 2011 Dec 6. PMID:22146051<ref>PMID:22146051</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tne" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida parapsilosis]]
[[Category: Large Structures]]
[[Category: Brynda J]]
[[Category: Dostal J]]
[[Category: Hruskova-Heidingsfeldova O]]
[[Category: Pachl P]]
[[Category: Pichova I]]
[[Category: Rezacova P]]