2fo8: Difference between revisions
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<StructureSection load='2fo8' size='340' side='right'caption='[[2fo8]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='2fo8' size='340' side='right'caption='[[2fo8]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fo8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2fo8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trycr Trycr]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FO8 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c34|2c34]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c34|2c34]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cha ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cha ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5693 TRYCR])</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=2fo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fo8 OCA], [https://pdbe.org/2fo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fo8 RCSB], [https://www.ebi.ac.uk/pdbsum/2fo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fo8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 11:28, 10 November 2021
Solution structure of the Trypanosoma cruzi cysteine protease inhibitor chagasinSolution structure of the Trypanosoma cruzi cysteine protease inhibitor chagasin
Structural highlights
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 PubMedA Trypanosoma cruzi cysteine protease inhibitor, termed chagasin, is the first characterized member of a new family of tight-binding cysteine protease inhibitors identified in several lower eukaryotes and prokaryotes but not present in mammals. In the protozoan parasite T.cruzi, chagasin plays a role in parasite differentiation and in mammalian host cell invasion, due to its ability to modulate the endogenous activity of cruzipain, a lysosomal-like cysteine protease. In the present work, we determined the solution structure of chagasin and studied its backbone dynamics by NMR techniques. Structured as a single immunoglobulin-like domain in solution, chagasin exerts its inhibitory activity on cruzipain through conserved residues placed in three loops in the same side of the structure. One of these three loops, L4, predicted to be of variable length among chagasin homologues, is flexible in solution as determined by measurements of (15)N relaxation. The biological implications of structural homology between chagasin and other members of the immunoglobulin super-family are discussed. Solution structure and backbone dynamics of the Trypanosoma cruzi cysteine protease inhibitor chagasin.,Salmon D, do Aido-Machado R, Diehl A, Leidert M, Schmetzer O, de A Lima AP, Scharfstein J, Oschkinat H, Pires JR J Mol Biol. 2006 Apr 14;357(5):1511-21. Epub 2006 Feb 3. PMID:16490204[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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