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Solution structure and backbone dynamics of the Trypanosoma cruzi cysteine protease inhibitor chagasin.
J Mol Biol. 2006 Apr 14; 357(5):1511-21.JM

Abstract

A 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.

Authors+Show Affiliations

Salmon D
Instituto de Bioquímica Médica, CCS, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowiski s/n, Rio de Janeiro, RJ 21941-590, Brazil.
do Aido-Machado R
No affiliation info available
Diehl A
No affiliation info available
Leidert M
No affiliation info available
Schmetzer O
No affiliation info available
de A Lima AP
No affiliation info available
Scharfstein J
No affiliation info available
Oschkinat H
No affiliation info available
Pires JR
No affiliation info available

MeSH

Amino Acid SequenceAnimalsCystatinsCysteine EndopeptidasesCysteine Proteinase InhibitorsHumansMolecular Sequence DataMolecular StructureNuclear Magnetic Resonance, BiomolecularProtein FoldingProtein Structure, TertiaryProtozoan ProteinsSequence AlignmentTrypanosoma cruzi

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16490204

Citation

Salmon, Didier, et al. "Solution Structure and Backbone Dynamics of the Trypanosoma Cruzi Cysteine Protease Inhibitor Chagasin." Journal of Molecular Biology, vol. 357, no. 5, 2006, pp. 1511-21.
Salmon D, do Aido-Machado R, Diehl A, et al. Solution structure and backbone dynamics of the Trypanosoma cruzi cysteine protease inhibitor chagasin. J Mol Biol. 2006;357(5):1511-21.
Salmon, D., do Aido-Machado, R., Diehl, A., Leidert, M., Schmetzer, O., de A Lima, A. P., Scharfstein, J., Oschkinat, H., & Pires, J. R. (2006). Solution structure and backbone dynamics of the Trypanosoma cruzi cysteine protease inhibitor chagasin. Journal of Molecular Biology, 357(5), 1511-21.
Salmon D, et al. Solution Structure and Backbone Dynamics of the Trypanosoma Cruzi Cysteine Protease Inhibitor Chagasin. J Mol Biol. 2006 Apr 14;357(5):1511-21. PubMed PMID: 16490204.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Solution structure and backbone dynamics of the Trypanosoma cruzi cysteine protease inhibitor chagasin. AU - Salmon,Didier, AU - do Aido-Machado,Rodolpho, AU - Diehl,Anne, AU - Leidert,Martina, AU - Schmetzer,Oliver, AU - de A Lima,Ana P C, AU - Scharfstein,Julio, AU - Oschkinat,Hartmut, AU - Pires,José R, Y1 - 2006/02/03/ PY - 2005/10/27/received PY - 2006/01/13/revised PY - 2006/01/17/accepted PY - 2006/2/24/pubmed PY - 2006/6/8/medline PY - 2006/2/24/entrez SP - 1511 EP - 21 JF - Journal of molecular biology JO - J Mol Biol VL - 357 IS - 5 N2 - A 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. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/16490204/Solution_structure_and_backbone_dynamics_of_the_Trypanosoma_cruzi_cysteine_protease_inhibitor_chagasin_ DB - PRIME DP - Unbound Medicine ER -