CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF VIPOXIN, A COMPLEX BETWEEN A TOXIC PHOSPHOLIPASE-A2 AND ITS NATURAL POLYPEPTIDE INHIBITOR

被引：9

作者：

BETZEL, C

VISANJI, M

WILSON, KS

GENOV, N

MANCHEVA, I

ALEKSIEV, B

SINGH, T

机构：

[1] BULGARIAN ACAD SCI, INST ORGAN CHEM, BU-1040 SOFIA, BULGARIA

[2] TECHNOL UNIV SOFIA, SOFIA, BULGARIA

[3] ALL INDIA INST MED SCI, DEPT BIOPHYS, NEW DELHI 110020, INDIA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 231卷 / 02期

关键词：

TOXIN; PHOSPHOLIPASE-A2; PHOSPHOLIPASE INHIBITOR; CRYSTALLIZATION; X-RAY ANALYSIS;

D O I：

10.1006/jmbi.1993.1297

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 toxin vipoxin, which is a complex between a basic toxic phospholipase A2 and an acidic non-toxic protein inhibitor, is found in the venom of the Bulgarian viper (Vipera ammodytes ammodytes), the most toxic snake in Europe. The two polypeptide chains each consist of 122 residues and are highly homologous (62%). The vipoxin complex is the first reported example of a high degree of structural homology between an enzyme and its natural inhibitor. The present crystals diffract in the X-ray beam to 1.8 Å resolution. The space group is P212121. The cell dimensions are a = 45.80 Å, b = 55.36 Å and c = 107.69 Å. Native data to a resolution of 2.8 Å have been recorded. © 1993 Academic Press, Inc.

引用

页码：498 / 500

页数：3

共 20 条

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