Human Eosinophil Major Basic Protein 2: Location of Disulfide Bonds and Free Sulfhydryl Groups |
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| Authors: | Lori A Wagner Lyo E Ohnuki Krishna Parsawar Gerald J Gleich Chad C Nelson |
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| Institution: | (1) Department of Dermatology, School of Medicine, University of Utah, Room 4R122 SOM 30 North 1900 East, Salt Lake City, Utah 84132, USA;(2) Mass Spectrometry and Proteomics Core Facility, University of Utah, Salt Lake City, Utah 84132, USA;(3) Department of Medicine, School of Medicine, University of Utah, Salt Lake City, Utah 84132, USA |
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| Abstract: | Eosinophil granule major basic protein 2 (MBP2 or major basic protein homolog) is a paralog of major basic protein (MBP1)
and, similar to MBP1, is cytotoxic and cytostimulatory in vitro. MBP2, a small protein of 13,433 Da molecular weight, contains
10 cysteine residues. Mass spectrometry shows two cystine disulfide linkages (Cys20–Cys115 and Cys92–Cys107) and 6 cysteine residues with free sulfhydryl groups (Cys2, Cys23, Cys42, Cys43, Cys68, and Cys96). MBP2, similar to MBP1, has conserved motifs in common with C-type lectins. The disulfide bond locations are conserved among
human MBP1, MBP2 and C-type lectins. |
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| Keywords: | Eosinophil major basic protein disulfide bonds C-type lectin |
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