Human eosinophil major basic protein 2: Location of disulfide bonds and free sulfhydryl groups

被引:4
|
作者
Wagner, Lori A.
Ohnuki, Lyo E.
Parsawar, Krishna
Gleich, Gerald J.
Nelson, Chad C.
机构
[1] Univ Utah, Sch Med, Dept Dermatol, Salt Lake City, UT 84132 USA
[2] Univ Utah, Mass Spectrometry & Proteom Core Facil, Salt Lake City, UT 84132 USA
[3] Univ Utah, Sch Med, Dept Med, Salt Lake City, UT 84132 USA
来源
PROTEIN JOURNAL | 2007年 / 26卷 / 01期
关键词
eosinophil; major basic protein; disulfide bonds; C-type lectin;
D O I
10.1007/s10930-006-9035-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (Cys(20)-Cys(115) and Cys(92)-Cys(107)) and 6 cysteine residues with free sulfhydryl groups (Cys(2), Cys(23), Cys(42), Cys(43), Cys(68), and Cys(96)). 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.
引用
收藏
页码:13 / 18
页数:6
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