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微管相关蛋白4结构模型。通过比较人类、小鼠和牛的序列定义的结构域。

A model for microtubule-associated protein 4 structure. Domains defined by comparisons of human, mouse, and bovine sequences.

作者信息

West R R, Tenbarge K M, Olmsted J B

机构信息

Department of Biology, University of Rochester, New York 14627.

出版信息

J Biol Chem. 1991 Nov 15;266(32):21886-96.

PMID:1718985
Abstract

cDNAs encoding human and mouse microtubule-associated protein 4 (MAP 4) were isolated. MAP 4 is encoded by a single gene. Multiple MAP 4 mRNAs are transcribed that are differentially expressed among mouse tissues. Open reading frames for the human and mouse MAP 4 clones indicate three distinct regions consisting of related sequences with different motifs. Approximately 30% of the protein is tandem related repeats of approximately 14 amino acids. Another region contains clusters of serine and proline. Four 18-mer repeats characteristic of the microtubule-binding domains of MAP 2 and tau are located at the carboxyl-terminal portion of MAP 4. Amino acid sequence analysis revealed that human and mouse MAP 4 are homologs of the bovine 190-kDa MAP/MAP U (Aizawa, H., Emori, Y., Murofushi, H., Kawasakai, H., Sakai, H., and Suzuki, K. (1990) J. Biol. Chem. 265, 13849-13855). Mouse and human MAP 4 and the bovine 190-kDa MAP are approximately 75% similar, indicating that these proteins are all members of the same class. Domains with extremely high conservation (greater than or equal to 88%) are: 1) the extreme amino terminus; 2) a proline-rich region between the KDM and S,P domains; 3) the microtubule-binding domain; and 4) the extreme carboxyl terminus.

摘要

编码人和小鼠微管相关蛋白4(MAP 4)的cDNA被分离出来。MAP 4由单个基因编码。转录出多种MAP 4 mRNA,它们在小鼠组织中差异表达。人和小鼠MAP 4克隆的开放阅读框表明有三个不同区域,由具有不同基序的相关序列组成。大约30%的蛋白质是约14个氨基酸的串联相关重复序列。另一个区域含有丝氨酸和脯氨酸簇。MAP 2和tau的微管结合结构域特有的四个18聚体重复序列位于MAP 4的羧基末端部分。氨基酸序列分析表明,人和小鼠的MAP 4是牛190 kDa MAP/MAP U的同源物(相泽浩、江守洋、室伏史、川崎浩、酒井浩和铃木健(1990年)《生物化学杂志》265卷,13849 - 13855页)。小鼠和人的MAP 4以及牛190 kDa MAP大约有75%的相似性,表明这些蛋白质都是同一类的成员。具有极高保守性(大于或等于88%)的结构域是:1)极端氨基末端;2)KDM和S、P结构域之间的富含脯氨酸区域;3)微管结合结构域;4)极端羧基末端。

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