The protease inhibitor chagasin of Trypanosoma cruzi adopts an immunoglobulin‐type fold and may have arisen by horizontal gene transfer

FEBS Letters

Grossi de Sá, M.Fatima¹  Rigden, Daniel J¹  Monteiro, Ana C.S¹ 

[1] National Centre of Genetic Resources and Biotechnology, Cenargen/Embrapa, S.A.I.N. Parque Rural, Final W5 Norte, 70770-900 Brasilia, Brazil

关键词: Chagasin;    Protease inhibitor;    Immunoglobulin-like domain;    Threading;    Horizontal gene transfer;    Trypanosoma cruzi;   

DOI  :  10.1016/S0014-5793(01)02753-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chagasin, a protein from Trypanosoma cruzi, is the first member of a new family of cysteine protease inhibitors. Despite its lack of significant sequence identity with known proteins, convincing structural models, using variable light chain templates, could be constructed on the basis of threading results. Experimental support for the final structure came from inhibition data for overlapping oligopeptides spanning the chagasin sequence. Chagasin therefore exemplifies a new protease inhibitor structural class and a new natural use for an immunoglobulin-like domain. Limited sequence resemblance suggests that chagasin may represent the result of a rare horizontal gene transfer from host to parasite.

【 授权许可】

Unknown