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Title: | Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed α-helix |
Authors: | Pereira, Pedro José Barbosa; Vega, María Cristina ![]() ![]() ![]() ![]() |
Keywords: | immunosuppressive agent protozoal protein tacrolimus virulence factor cyclophilin |
Issue Date: | 2002 |
Publisher: | Nature Publishing Group |
Citation: | EMBO Reports 3(1): 88-94 (2002) |
Abstract: | The macrophage infectivity potentiator protein from Trypanosoma cruzi (TcMIP) is a major virulence factor secreted by the etiological agent of Chagas' disease. It is functionally involved in host cell invasion. We have determined the three-dimensional crystal structure of TcMIP at 1.7 Å resolution. The monomeric protein displays a peptidyl-prolyl cis-trans isomerase (PPlase) core, encompassing the characteristic rotamase hydrophobic active site, thus explaining the strong inhibition of TcMIP by the immunosuppressant FK506 and related drugs. In TcMIP, the twisted β-sheet of the core is extended by an extra β-strand, preceded by a long, exposed N-terminal α-helix, which might be a target recognition element. An invasion assay shows that the MIP protein from Legionella pneumophila (LpMIP), which has an equivalent N-terminal α-helix, can substitute for TcMIP. An additional exposed α-helix, this one unique to TcMIP, is located in the C-terminus of the protein. The high-resolution structure reported here opens the possibility for the design of new inhibitory drugs that might be useful for the clinical treatment of American trypanosomiasis. |
Publisher version (URL): | http://dx.doi.org/10.1093/embo-reports/kvf009 |
URI: | http://hdl.handle.net/10261/107911 |
DOI: | http://dx.doi.org/10.1093/embo-reports/kvf009 |
Identifiers: | doi: 10.1093/embo-reports/kvf009 issn: 1469-221X |
Appears in Collections: | (IPBLN) Artículos (IBMB) Artículos |
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