Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution

被引：18

作者：

Wakasugi, K ^{[1
]}

Morishima, I

机构：

[1] Kyoto Univ, Grad Sch Engn, Dept Mol Engn, Kyoto 6158510, Japan

[2] PRESTO, Japan Sci & Technol Agcy, Kawaguchi, Saitama 3320012, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 330卷 / 02期

关键词：

neuroglobin; module substitution; heme environmental structure; secondary structure; protein stability;

D O I：

10.1016/j.bbrc.2005.03.021

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：

Neuroglobin (Ngb) is a recently discovered vertebrate heme protein that can reversibly bind oxygen that is expressed in the brain. Zebratish and human Ngb share about 50% amino acid sequence identity. These Ngb proteins consist of four compact protein structural unit "modules" referred to as M1-M4. In the present study, we investigated the effects of module substitution on the properties of Ngb. Specifically, we prepared and characterized a chimeric ZHZZ Ngb in which the heme-binding module M2 of zebrafish Ngb was replaced by the comparable human Ngb module. Our results showed that the chimeric ZHZZ was stable and formed almost the identical heme-environmental and alpha-helical Structure as the human and zebrafish Ngb proteins, suggesting that the structure of Ngb has been evolutionarily conserved. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：591 / 597

页数：7

共 25 条

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