EVIDENCE FOR THE INVOLVEMENT OF TYPE-II DOMAINS IN COLLAGEN BINDING BY 72-KDA TYPE-IV PROCOLLAGENASE

被引：69

作者：

BANYAI, L ^{[1
]}

PATTHY, L ^{[1
]}

机构：

[1] HUNGARIAN ACAD SCI,BIOL RES CTR,INST ENZYMOL,POB 7,H-1518 BUDAPEST,HUNGARY

来源：

FEBS LETTERS | 1991年 / 282卷 / 01期

关键词：

TYPE-IV COLLAGENASE; FIBRONECTIN; MATRIX DEGRADATION; TISSUE REMODELING; TUMOR INVASION;

D O I：

10.1016/0014-5793(91)80436-7

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 fibronectin-related region of the 72 kDa type IV procollagenase has been expressed in E. coli as a beta-galactosidase fusion product. The fragment containing the three type II units of the protein was found to have affinity for denatured collagen, suggesting that these domains may be responsible for the collagen-affinity of type IV collagenase. We have also shown that segment Ala-Ala-His-Glu of type IV collagenase (residues 372-375), which is similar to a fibronectin-segment previously implicated in collagen-binding, is not essential for binding activity.

引用

页码：23 / 25

页数：3

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