Functional consequences of disulfide bond formation in gelsolin

被引:19
作者
Allen, PG
机构
[1] Division of Experimental Medicine, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115
关键词
gelsolin; protein structure; disulfide bond; calcium binding protein; actin binding protein;
D O I
10.1016/S0014-5793(96)01439-1
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
Gelsolin is an actin monomer binding and filament severing protein synthesized in plasma and cytoplasmic forms differing by an N-terminal amino acid extension and a disulfide bond between Cys-188 and Cys-201. To determine whether this bond altered gelsolin regulation or function, oxidized and reduced plasma gelsolins were assayed for severing, monomer binding and nucleation activity at a variety of rate-limiting calcium concentrations. The results indicate that the disulfide bond in domain 2 of gelsolin influences the transmission of information from C-terminal regulatory sites to functional sites in the N-terminus.
引用
收藏
页码:89 / 94
页数:6
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