Horiuchi R, Yamauchi K
Department of Pharmacy, Gunma University School of Medicine.
Nihon Rinsho. 1994 Apr;52(4):890-5.
The protein or cDNA sequencing revealed that the membrane-associated 3,5,3'-triiodo-thyronine binding protein (T3BP) acts as a multifunctional protein:protein disulfide isomerase (PDI) catalyzing isomerization of intra- and inter-molecular disulfide bridge in the proteins, beta-subunit of prolyl 4-hydroxylase catalyzing the formation of 4-hydroxyproline in collagen molecules, glycosylation site binding protein which is a component of oligosaccharyl transferase transferring oligosaccharide chains to the asparagine residues of Asn-X-Ser/Thr site in nascent polypeptide, and a component of triglyceride transfer protein complex involved in the transfer unit of triglyceride, cholesteryl ester and phosphatidylcholine between biomembranes. The functions of 55 k-T3BP/PDI, mainly involved in important post-translational modifications, are discussed in relation to the domain structure of the molecule.
蛋白质或cDNA测序显示，膜相关的3,5,3'-三碘甲状腺原氨酸结合蛋白（T3BP）是一种多功能蛋白：作为蛋白质二硫键异构酶（PDI），催化蛋白质分子内和分子间二硫键的异构化；作为脯氨酰4-羟化酶的β亚基，催化胶原蛋白分子中4-羟脯氨酸的形成；作为糖基化位点结合蛋白，是寡糖基转移酶的一个组分，将寡糖链转移至新生多肽中Asn-X-Ser/Thr位点的天冬酰胺残基上；作为甘油三酯转移蛋白复合物的一个组分，参与生物膜之间甘油三酯、胆固醇酯和磷脂酰胆碱的转移单元。本文结合该分子的结构域结构，讨论了主要参与重要翻译后修饰的55k-T3BP/PDI的功能。
