DROSOPHILA KELCH MOTIF IS DERIVED FROM A COMMON ENZYME FOLD

被引：167

作者：

BORK, P

DOOLITTLE, RF

机构：

[1] MAX DELBRUCK CTR MOLEC MED,D-13125 BERLIN,GERMANY

[2] UNIV CALIF SAN DIEGO,CTR MOLEC GENET,LA JOLLA,CA 92093

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 236卷 / 05期

基金：

美国国家卫生研究院;

关键词：

PROTEIN MODULES; HOMOLOGY; PROPELLER FOLD; GALACTOSE OXIDASE; KELCH MOTIF;

D O I：

10.1016/0022-2836(94)90056-6

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：

A systematic screening of sequence databases with a motif hitherto found only in animal and poxvirus proteins has revealed a trail leading back to prokaryotes. Fortuitously, an X-ray structure is available for one of the identified sequences and shows the fundamental fold to be a set of circularly arranged β sheets. This structure may be very widely distributed throughout the biological world in sialidases and some other enzymes. In bacteria, a mobile noncatalytic domain is often associated with these same enzymes. © 1994.

引用

页码：1277 / 1282

页数：6

共 40 条

[1] 3,400 NEW EXPRESSED SEQUENCE TAGS IDENTIFY DIVERSITY OF TRANSCRIPTS IN HUMAN BRAIN [J].