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白细胞黏附蛋白β亚基的克隆:与细胞外基质受体的同源性定义了一个新的超基因家族。

Cloning of the beta subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family.

作者信息

Kishimoto T K, O'Connor K, Lee A, Roberts T M, Springer T A

出版信息

Cell. 1987 Feb 27;48(4):681-90. doi: 10.1016/0092-8674(87)90246-7.

Abstract

We have isolated cDNA clones encoding the beta subunit of the human LFA-1, Mac-1, and p150,95 family of leukocyte adhesion proteins. The deduced 769-amino-acid sequence defines a cysteine-rich polypeptide with the characteristic features of an integral membrane protein. Peptide sequence data, Northern blot analysis, and Southern blot analysis suggest that a single gene encodes the beta subunit of all three leukocyte adhesion proteins. There is 45% homology between the beta subunit sequence and band III of integrin, a chick fibronectin and laminin receptor. This homology defines a new supergene family of cellular adhesion proteins.

摘要

我们已经分离出编码人白细胞粘附蛋白LFA-1、Mac-1和p150,95家族β亚基的cDNA克隆。推导的769个氨基酸序列定义了一种富含半胱氨酸的多肽,具有整合膜蛋白的特征。肽序列数据、Northern印迹分析和Southern印迹分析表明,单个基因编码所有三种白细胞粘附蛋白的β亚基。β亚基序列与整联蛋白的带III(一种鸡纤连蛋白和层粘连蛋白受体)之间有45%的同源性。这种同源性定义了一个新的细胞粘附蛋白超基因家族。

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