View source for 6cjz


==Solution Structure of Amebosin==
<StructureSection load='6cjz' size='340' side='right'caption='[[6cjz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cjz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CJZ FirstGlance]. <br>
</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=6cjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cjz OCA], [https://pdbe.org/6cjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cjz RCSB], [https://www.ebi.ac.uk/pdbsum/6cjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cjz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ICP1_ENTHI ICP1_ENTHI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The genome of Entamoeba histolytica encodes approximately 50 Cysteine Proteases (CPs) whose activity is regulated by two Inhibitors of Cysteine Proteases (ICPs), EhICP1 and EhICP2. The main difference between both EhICPs is the acquisition of a 17 N-terminal targeting signal in EhICP2 and three exposed cysteine residues in EhICP1. The three exposed cysteines in EhICP1 potentiate the formation of cross-linking species that drive heterogeneity. Here we solved the NMR structure of EhICP1 using a mutant protein without accessible cysteines. Our structural data shows that EhICP1 adopts an immunoglobulin fold composed of seven beta-strands, and three solvent exposed loops that resemble the structures of EhICP2 and chagasin. EhICP1 and EhICP2 are able to inhibit the archetypical cysteine protease papain by intercalating their BC loops into the protease active site independently of the character of the residue (serine or threonine) responsible to interact with the active site of papain. EhICP1 and EhICP2 present signals of functional divergence as they clustered in different clades. Two of the three exposed cysteines in EhICP1 are located at the DE loop that intercalates into the CP substrate-binding cleft. We propose that the solvent exposed cysteines of EhICP1 play a role in regulating its inhibitory activity and that in oxidative conditions, the cysteines of EhICP1 react to form intra and intermolecular disulfide bonds that render an inactive inhibitor. EhICP2 is not subject to redox regulation, as this inhibitor does not contain a single cysteine residue. This proposed redox regulation may be related to the differential cellular localization between EhICP1 and EhICP2.

Solution structure of the inhibitor of cysteine proteases 1 from Entamoeba histolytica reveals a possible auto regulatory mechanism.,Flores-Solis D, Mendoza A, Renteria-Gonzalez I, Casados-Vazquez LE, Trasvina-Arenas CH, Jimenez-Sandoval P, Benitez-Cardoza CG, Del Rio-Portilla F, Brieba LG Biochim Biophys Acta Proteins Proteom. 2020 Jul 28;1868(11):140512. doi:, 10.1016/j.bbapap.2020.140512. PMID:32731033<ref>PMID:32731033</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6cjz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Entamoeba histolytica]]
[[Category: Large Structures]]
[[Category: Brieba de Castro L]]
[[Category: Del Rio Portilla F]]
[[Category: Flores-Solis D]]
[[Category: Mendoza A]]