The lysine cluster in the collagen-like domain of the scavenger receptor provides for its ligand binding and ligand specificity

被引:31
作者
Yamamoto, K
Nishimura, N
Doi, T
Imanishi, T
Kodama, T
Suzuki, K
Tanaka, T
机构
[1] BIOMOL ENGN RES INST,SUITA,OSAKA 565,JAPAN
[2] KANEBO LTD,NEW DRUG DISCOVERY RES LAB,MIYAKOJIMA KU,OSAKA 534,JAPAN
[3] OSAKA UNIV,FAC PHARMACEUT SCI,SUITA,OSAKA 565,JAPAN
[4] UNIV TOKYO,ADV SCI & TECHNOL RES CTR,DEPT MOL BIOL & MED,MEGURO KU,TOKYO 113,JAPAN
关键词
scavenger receptor; collagen-like domain; inhibitor; binding assay; lysine cluster;
D O I
10.1016/S0014-5793(97)01006-5
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
Scavenger receptors bind modified low-density lipoproteins (LDL) on a collagen-like domain which possesses a lysine cluster at the carboxy end, We previously constructed a receptor model peptide containing the lysine cluster, In the present study, we evaluated the ligand specificity of the receptor model peptide. It selectively bound modified-LDLs, and not LDL. The binding of acetylated-LDL (Ac-LDL) was inhibited by dextran sulfate, fucoidan, and sulfatides in a manner similar to that of the natural receptor, Both polyguanylic and polyinosinic acids inhibit the Ac-LDL binding whereas polycytidylic acid did not, These results indicate that the lysine cluster in the collagen-like domain has important roles in both ligand binding and ligand specificity. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:182 / 186
页数:5
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