Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain

被引:118
作者
Liang, ZC
SottrupJensen, L
Aspan, A
Hall, M
Soderhall, K
机构
[1] UPPSALA UNIV, DEPT PHYSIOL BOT, S-75236 UPPSALA, SWEDEN
[2] AARHUS UNIV, DEPT BIOL MOL & STRUCT, DK-8000 AARHUS C, DENMARK
关键词
D O I
10.1073/pnas.94.13.6682
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
A 155-kDa proteinase inhibitor, pacifastin, from plasma of the freshwater crayfish, Pacifastacus leniusculus, was found to be composed of two covalently linked subunits, The two subunits are encoded by two different mRNAs, which were cloned and sequenced, The hear: chain of pacifastin (105 kDa) is related to transferrins, containing three transferrin lobes, two of which seem to be active for iron binding, The light chain of pacifastin (44 kDa) is the inhibitory subunit, and has nine cysteine-rich inhibitory domains that are homologous to each other and to low molecular weight proteinase inhibitors isolated from the grasshopper, Locusta migratoria. The nine light chain domains and the Locusta inhibitors share a characteristic cysteine array (Cys-Xaa(9-12)-Cys-Xaa(2)-Cys-Xaa-Cys-Xaa(6-delta)-Cys-Xaa(4)-Cys) distinct from any described proteinase inhibitor family, suggesting that they constitute a new family of proteinase inhibitors, Pacifastin is the first known protein that has combined properties of a transferrin-like molecule and a proteinase inhibitor.
引用
收藏
页码:6682 / 6687
页数:6
相关论文
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