NETROPSIN, A DNA-BINDING OLIGOPEPTIDE STRUCTURAL AND BINDING STUDIES

被引：124

作者：

BERMAN, HM

NEIDLE, S

ZIMMER, C

THRUM, H

机构：

[1] UNIV LONDON,KINGS COLL,DEPT BIOPHYS,LONDON WC2B 5RL,ENGLAND

[2] AKAD WISSENSCH DDR,MOLEK BIOL & MED FORSCHUNGSZENTRUM,ZENT INST MIKROBIOL & EXPTL THERAPIE,DDR-69 JENA,GER DEM REP

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 561卷 / 01期

基金：

美国国家卫生研究院;

关键词：

(Structure); Antibiotic; DNA-binding oligopeptide; Netropsin; X-ray crystallography;

D O I：

10.1016/0005-2787(79)90496-9

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 crystal structure of netropsin, an oligopeptide which binds to DNA, has been determined. The molecule is bowed with the amide groups on the concave side, and the carbonyl and methyl groups on the convex side. The amide groups participate in extensive hydrogen bonding with water molecules; the charged amino end groups interact with the sulfate anions. Binding of netropsin to poly(dA) · poly(dT) under conditions of different ionic strength was also studied. Utilizing the crystallographic as well as the binding data, it is possible to build a model which explains the specificity of this antibiotic. © 1979.

引用

页码：124 / 131

页数：8

共 12 条

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