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==High Resolution Crystal Structure Analysis Of Cruzain non-covalently Bound To A Hydroxymethyl Ketone Inhibitor (I)== | ==High Resolution Crystal Structure Analysis Of Cruzain non-covalently Bound To A Hydroxymethyl Ketone Inhibitor (I)== | ||
<StructureSection load='1me4' size='340' side='right' caption='[[1me4]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='1me4' size='340' side='right'caption='[[1me4]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1me4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1me4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ME4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ME4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=T10:[1-(1-BENZYL-3-HYDROXY-2-OXO-PROPYLCARBAMOYL)-2-PHENYL-ETHYL]-CARBAMIC+ACID+BENZYL+ESTER'>T10</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1me4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1me4 OCA], [https://pdbe.org/1me4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1me4 RCSB], [https://www.ebi.ac.uk/pdbsum/1me4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1me4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CYSP_TRYCR CYSP_TRYCR] Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group. The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/me/1me4_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/me/1me4_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 29: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 1me4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1me4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cruzain|Cruzain]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Trypanosoma cruzi]] | ||
[[Category: | [[Category: Brinen LS]] | ||
[[Category: | [[Category: Ellman JA]] | ||
[[Category: | [[Category: Huang L]] | ||
Latest revision as of 12:38, 25 December 2024
High Resolution Crystal Structure Analysis Of Cruzain non-covalently Bound To A Hydroxymethyl Ketone Inhibitor (I)High Resolution Crystal Structure Analysis Of Cruzain non-covalently Bound To A Hydroxymethyl Ketone Inhibitor (I)
Structural highlights
FunctionCYSP_TRYCR Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group. The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle. 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 PubMedThe crystal structures of two hydroxymethyl ketone inhibitors complexed to the cysteine protease cruzain have been determined at 1.1 and 1.2 A resolution, respectively. These high resolution crystal structures provide the first structures of non-covalent inhibitors bound to cruzain. A series of compounds were prepared and tested based upon the structures providing further insight into the key binding interactions. Crystal structures of reversible ketone-Based inhibitors of the cysteine protease cruzain.,Huang L, Brinen LS, Ellman JA Bioorg Med Chem. 2003 Jan 2;11(1):21-9. PMID:12467703[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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