a two disulfide bridge kazal domain from phytophthora exhibits stable inhibitory activity against serine proteases of the subtilisin family两个二硫桥kazal域从疫霉展品稳定对枯草杆菌蛋白酶家族的丝氨酸蛋白酶抑制活性.pdfVIP

BMC Biochemistry BioMed Central Research article Open Access A two disulfide bridge Kazal domain from Phytophthora exhibits stable inhibitory activity against serine proteases of the subtilisin family Miaoying Tian and Sophien Kamoun* Address: Department of Plant Pathology, The Ohio State University, Ohio Agricultural Research and Development Center, Wooster, OH 44691, USA Email: Miaoying Tian - mt326@; Sophien Kamoun* - kamoun.1@ * Corresponding author Published: 23 August 2005 Received: 08 April 2005 Accepted: 23 August 2005 BMC Biochemistry 2005, 6:15 doi:10.1186/1471-2091-6-15 This article is available from: /1471-2091/6/15 © 2005 Tian and Kamoun; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: Kazal-like serine protease inhibitors are defined by a conserved sequence motif. A typical Kazal domain contains six cysteine residues leading to three disulfide bonds with a 1–5/2– 4/3–6 pattern. Most Kazal domains described so far belong to this class. However, a novel class of Kazal domains with two disulfide bridges resulting from the absence of the third and sixth cysteines have been found in biologically important molecules, such as human LEKTI, a 15-domain inhibitor associated with the severe congenital disease Netherton syndrome. These