Solution Structure and Backbone Dynamics of the Trypanosoma cruzi Cysteine Protease Inhibitor Chagasin

Solution Structure and Backbone Dynamics of the Trypanosoma cruzi Cysteine Protease Inhibitor Chagasin

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 r...

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Bibliographic Details
Published in:Journal of molecular biology Vol. 357; no. 5; pp. 1511 - 1521
Main Authors: Salmon, Didier, do Aido-Machado, Rodolpho, Diehl, Anne, Leidert, Martina, Schmetzer, Oliver, de A. Lima, Ana P.C., Scharfstein, Julio, Oschkinat, Hartmut, Pires, José R.
Format: Journal Article
Language:English
Published: England Elsevier Ltd 14-04-2006
Subjects:
Amino Acid Sequence
Animals
chagasin
Cystatins - chemistry
Cystatins - metabolism
Cysteine Endopeptidases - chemistry
Cysteine Endopeptidases - metabolism
cysteine protease inhibitors
Cysteine Proteinase Inhibitors - chemistry
Cysteine Proteinase Inhibitors - metabolism
dynamics
Humans
Molecular Sequence Data
Molecular Structure
NMR structure
Nuclear Magnetic Resonance, Biomolecular
Protein Folding
Protein Structure, Tertiary
Protozoan Proteins - chemistry
Protozoan Proteins - metabolism
Sequence Alignment
T. cruzi
Trypanosoma cruzi
Trypanosoma cruzi - chemistry
Trypanosoma cruzi - metabolism
NMR structure
CSP
NOE
T. cruzi
TOCSY
CP
dynamics
cysteine protease inhibitors
ICP
chagasin
NOESY
HSQC
Ig
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Summary: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 15N relaxation. The biological implications of structural homology between chagasin and other members of the immunoglobulin super-family are discussed.
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ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2006.01.064