3-DIMENSIONAL STRUCTURE OF ECHISTATIN, THE SMALLEST ACTIVE RGD PROTEIN

被引：208

作者：

SAUDEK, V ^{[1
]}

ATKINSON, RA ^{[1
]}

PELTON, JT ^{[1
]}

机构：

[1] MARION MERRELL DOW RES INST,16 RUE DANKARA,BP447-R9,F-67009 STRASBOURG,FRANCE

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 30期

关键词：

D O I：

10.1021/bi00244a003

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：

Echistatin is a 49 amino acid protein isolated from the venom of a viper (Echis carinatus) and is one of the smallest natural adhesive ligands that interacts with integrin-type receptors through an Arg-Gly-Asp (RGD) sequence. The structure of echistatin in aqueous solution has been determined by nuclear magnetic resonance spectroscopy. Nuclear Overhauser spectra yielded 490 interatomic distance constraints, which were used in distance geometry calculations. The chain is shown to fold in a series of irregular loops to form a rigid core stabilized by four cystine cross-links. From this core an irregular hairpin and the C-terminus protrude. The core and the hairpin are further stabilized by a network of hydrogen bonds. The RGD sequence is located in a mobile loop at the tip of the hairpin. The mobility and its significance for activity are discussed.

引用

页码：7369 / 7372

页数：4

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