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70 kDa过氧化物酶体膜蛋白是多药耐药(P-糖蛋白)相关ATP结合蛋白超家族的成员。

The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily.

作者信息

Kamijo K, Taketani S, Yokota S, Osumi T, Hashimoto T

机构信息

Department of Biochemistry, Shinshu University School of Medicine, Matsumoto, Japan.

出版信息

J Biol Chem. 1990 Mar 15;265(8):4534-40.

PMID:1968461
Abstract

The 70-kDa peroxisomal membrane protein (PMP70) is one of the major integral membrane proteins of rat liver peroxisomes. cDNA clones for PMP70 were isolated and sequenced. The predicted amino acid sequence (659 amino acid residues) revealed that the carboxyl-terminal region of PMP70 has strong sequence similarities to a group of ATP-binding proteins such as MalK and Mdr. These proteins form a superfamily and are involved in various biological processes including membrane transport. Limited protease treatment of peroxisomes showed that the ATP-binding domain of PMP70 is exposed to the cytosol. The hydropathy profile, in comparison with those of several other members of the ATP-binding protein superfamily, suggests that PMP70 is a transmembrane protein possibly forming a channel. Based on these results, we propose that PMP70 is involved in active transport across the peroxisomal membrane.

摘要

70 kDa的过氧化物酶体膜蛋白(PMP70)是大鼠肝脏过氧化物酶体的主要整合膜蛋白之一。分离并测序了PMP70的cDNA克隆。预测的氨基酸序列(659个氨基酸残基)显示,PMP70的羧基末端区域与一组ATP结合蛋白(如MalK和Mdr)具有很强的序列相似性。这些蛋白形成一个超家族,并参与包括膜运输在内的各种生物过程。对过氧化物酶体进行有限的蛋白酶处理表明,PMP70的ATP结合结构域暴露于细胞质中。与ATP结合蛋白超家族的其他几个成员相比,亲水性图谱表明PMP70是一种可能形成通道的跨膜蛋白。基于这些结果,我们提出PMP70参与过氧化物酶体膜的主动运输。

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