Interacting partners for kringle domains of plasminogen: Common binding with K1 and K5 domains

被引：0

作者：

Kong, N ^{[1
]}

Lim, D ^{[1
]}

Lee, K ^{[1
]}

机构：

[1] Sejong Univ, Dept Appl Chem, Seoul 143747, South Korea

来源：

PROTEIN AND PEPTIDE LETTERS | 2004年 / 11卷 / 06期

关键词：

angiostatin; kringles; yeast two hybrid;

D O I：

10.2174/0929866043406382

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：

We have identified MAZR and Rg12 as specific interacting partners for kringle domains in angiostatin (K1-4) and K5 using yeast two hybrid screening. Both K1 and K1-4 have strong interaction with MAZR and Rg12 whereas K5 only binds with Rg12. No interaction of K2, K3, and K4 with either of these binding proteins was detected. We Suggest that a common binding motif may exist near LBS-4 that is required for binding with Rg12 but not with MAZR.

引用

页码：521 / 525

页数：5

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