View source for 7age


==Protease Sapp1p from Candida parapsilosis in complex with KB32==
<StructureSection load='7age' size='340' side='right'caption='[[7age]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7age]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis Candida parapsilosis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AGE 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]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PSA:3-HYDROXY-4-AMINO-5-PHENYLPENTANOIC+ACID'>PSA</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=7age FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7age OCA], [https://pdbe.org/7age PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7age RCSB], [https://www.ebi.ac.uk/pdbsum/7age PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7age ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARP1_CANPA CARP1_CANPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic Candida albicans yeasts frequently cause infections in hospitals. Antifungal drugs lose effectiveness due to other Candida species and resistance. New medications are thus required. Secreted aspartic protease of C. parapsilosis (Sapp1p) is a promising target. We have thus solved the crystal structures of Sapp1p complexed to four peptidomimetic inhibitors. Three potent inhibitors (K(i): 0.1, 0.4, 6.6 nM) resembled pepstatin A (K(i): 0.3 nM), a general aspartic protease inhibitor, in terms of their interactions with Sapp1p. However, the weaker inhibitor (K(i): 14.6 nM) formed fewer nonpolar contacts with Sapp1p, similarly to the smaller HIV protease inhibitor ritonavir (K(i): 1.9 microM), which, moreover, formed fewer H-bonds. The analyses have revealed the structural determinants of the subnanomolar inhibition of C. parapsilosis aspartic protease. Because of the high similarity between Saps from different Candida species, these results can further be used for the design of potent and specific Sap inhibitor-based antimycotic drugs.

Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p from Candida parapsilosis.,Dostal J, Brynda J, Vankova L, Zia SR, Pichova I, Heidingsfeld O, Lepsik M J Enzyme Inhib Med Chem. 2021 Dec;36(1):914-921. doi: , 10.1080/14756366.2021.1906664. PMID:33843395<ref>PMID:33843395</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7age" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida parapsilosis]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Brynda J]]
[[Category: Dostal J]]
[[Category: Heidingsfeld O]]