Please use this identifier to cite or link to this item: https://doi.org/10.1017/S0031182002002329
Title: A male-specific (cysteine-rich) protein of Oesophagostomum dentatum (Strongylida) with structural characteristics of a serine protease inhibitor containing two trypsin inhibitor-like domains
Authors: Boag, P.R.
Ranganathan, S. 
Newton, S.E.
Gasser, R.B.
Keywords: Gender-specific expression
Oesophagostomum dentatum
Parasitic nematode
Serine protease inhibitor
Structural model
Trypsin inhibitor-like
Issue Date: 1-Nov-2002
Source: Boag, P.R.,Ranganathan, S.,Newton, S.E.,Gasser, R.B. (2002-11-01). A male-specific (cysteine-rich) protein of Oesophagostomum dentatum (Strongylida) with structural characteristics of a serine protease inhibitor containing two trypsin inhibitor-like domains. Parasitology 125 (5) : 445-455. ScholarBank@NUS Repository. https://doi.org/10.1017/S0031182002002329
Abstract: A cDNA was isolated from an adult male Oesophagostomum dentatum gene library by screening with a male-specific, partial expressed sequence tag (EST) probe identified previously using a differential display technique. The full-length cDNA of 642 bp included 5′ and 3′ untranslated regions of 44 and 121 nucleotides, respectively, and encoded a predicted protein with a putative 18 amino acid signal sequence and a mature polypeptide of 14.7 kDa comprising ∼ 15% cysteine residues. The amino acid sequence showed similarity with a number of proteins from Caenorhabditis elegans, parasitic nematodes, insects and amphibia, all of which contain a trypsin inhibitor-like cysteine-rich domain. A 3-dimensional structure model constructed for the O. dentatum protein (designated OdmCRP) inferred that it is composed of 2 domains, each with 5 disulfide bonds, which are indicative of the Ascaris family of serine protease inhibitors. These findings indicate that OdmCRP, with 2 structural domains relating to functionally active sites, is a new member of this inhibitor family.
Source Title: Parasitology
URI: http://scholarbank.nus.edu.sg/handle/10635/113330
ISSN: 00311820
DOI: 10.1017/S0031182002002329
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