Characterization of the interaction between beta(2)-glycoprotein I and calmodulin, and identification of a binding sequence in beta(2)-glycoprotein I

被引：7
|
作者：
Rojkjaer, R
Klaerke, DA
Schousboe, I
机构：
[1] UNIV COPENHAGEN,PANUM INST,DEPT MED BIOCHEM & GENET,DK-2200 COPENHAGEN N,DENMARK
[2] UNIV COPENHAGEN,PANUM INST,DEPT MED PHYSIOL,BIOMEMBRANE RES CTR,DK-2200 COPENHAGEN N,DENMARK
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1997年 / 1339卷 / 02期
关键词：
beta(2)-glycoprotein I; calmodulin; calmodulin-binding site;
D O I：
10.1016/S0167-4838(96)00234-8
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：
beta(2)-Glycoprotein I was shown to bind reversibly to calmodulin in a Ca2+-dependent manner with a 1:1 stoichiometry, a K-d of 3 x 10(-9) M and a Hill coefficient of 1.4. A sequence in beta(2)-glycoprotein I (Lys-Pro-Gly-Tyr-Val-Ser-Arg-Gly-Gly-Met-Arg-Lys-Phe-Ile-) limited by Cys-32 and Cys-47 is suggested to be the calmodulin-binding region. This sequence was the only one in beta(2)-glycoprotein I theoretically having the ability to form a basic amphiphilic alpha-helix typical of a calmodulin binding sequence. The peptide corresponding to this sequence was synthesized and found to inhibit the interaction between beta(2)-glycoprotein I and calmodulin with an IC50 value of 0.38 x [beta(2)-glycoprotein I] and to displace the beta(2)-glycoprotein I from the beta(2)-glycoprotein I/calmodulin complex with an IC50 value of 0.90 x [beta(2)-glycoprotein I].
引用
收藏
页码：217 / 225
页数：9
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