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视网膜环磷酸鸟苷磷酸二酯酶β亚基中γ亚基相互作用位点的鉴定。

Identification of the gamma-subunit interaction sites in the retinal cyclic-GMP phosphodiesterase beta-subunit.

作者信息

Oppert B, Takemoto D J

机构信息

Department of Biochemistry, Kansas State University, Manhattan 66506.

出版信息

Biochem Biophys Res Commun. 1991 Jul 31;178(2):474-9. doi: 10.1016/0006-291x(91)90131-p.

Abstract

Using synthetic peptides, the identification of the retinal cyclic-GMP phosphodiesterase (cGMP PDE) interaction sites for the inhibitory gamma-subunit in the catalytic alpha-subunit were recently localized to residues #16-30 and 78-90 in the alpha-subunit (1). In this study, a binding radioimmunoassay (RIA) showed a weak interaction between PDE gamma and PDE beta subunits in PDE beta residues #15-34, and stronger interaction sites were found in residues #91-110 and 211-230. Sequence comparison between PDE alpha and PDE beta illustrate some differences in these regions, particularly in PDE alpha 16-30 and PDE beta 15-34 regions. Differences in interaction sites in PDE alpha and PDE beta for PDE gamma may account for the differences in affinities observed between PDE gamma and the catalytic subunits.

摘要

利用合成肽,近期已将催化性α亚基中抑制性γ亚基与视网膜环磷酸鸟苷磷酸二酯酶(cGMP PDE)的相互作用位点定位至α亚基中的16 - 30号残基和78 - 90号残基(1)。在本研究中,一项结合放射免疫分析(RIA)显示,PDEγ与PDEβ亚基在PDEβ的15 - 34号残基间存在弱相互作用,且在91 - 110号残基和211 - 230号残基中发现了更强的相互作用位点。PDEα与PDEβ之间的序列比较表明这些区域存在一些差异,尤其是在PDEα的16 - 30区域和PDEβ的15 - 34区域。PDEγ与PDEα和PDEβ相互作用位点的差异可能解释了PDEγ与催化亚基之间观察到的亲和力差异。

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