PURIFICATION AND STRUCTURAL CHARACTERIZATION OF THE CD11B/CD18 INTEGRIN ALPHA-SUBUNIT-I DOMAIN REVEALS A FOLDED CONFORMATION IN SOLUTION

被引：7

作者：

FAIRBANKS, MB ^{[1
]}

POLLOCK, JR ^{[1
]}

PRAIRIE, MD ^{[1
]}

SCAHILL, TA ^{[1
]}

BACZYNSKYJ, L ^{[1
]}

HEINRIKSON, RL ^{[1
]}

STOCKMAN, BJ ^{[1
]}

机构：

[1] UPJOHN CO,UPJOHN LABS,KALAMAZOO,MI 49007

来源：

FEBS LETTERS | 1995年 / 369卷 / 2-3期

关键词：

ADHESION BIOLOGY; CIRCULAR DICHROISM; FUSION PROTEIN; I DOMAIN; INTEGRIN; PROTEIN NMR;

D O I：

10.1016/0014-5793(95)00747-W

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The alpha subunits of the leukocyte CD11/CD18 integrins contain a similar to 200 amino acid 'inserted' or I domain. The I domain of the cell-surface Mac-1 (CD11b/CD18) integrin has been shown to be the major recognition site for several adhesion ligands, including iC3b, fibrinogen, factor,X, and ICAM-1. The I domain from the Mac-1 alpha subunit has been expressed in Escherichia coli as a soluble GST-fusion protein containing a factor X(a) sensitive cleavage site. Analytical characterization of the purified I domain reveals that it is obtained in very high quality at high yields. CD and NMR spectra indicate that I domain adopts a predominantly folded structure in solution, independent of the remainder of the alpha subunit. addition of Ca2+ and Mg2+ did not significantly perturb the structural conformation.

引用

页码：197 / 201

页数：5

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