A POSSIBLE REGULATION OF NEGATIVE FACTOR (NEF) ACTIVITY OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 BY THE VIRAL PROTEASE

被引：51

作者：

FREUND, J

KELLNER, R

KONVALINKA, J

WOLBER, V

KRAUSSLICH, HG

KALBITZER, HR

机构：

[1] MAX PLANCK INST MED RES,DEPT BIOPHYS,D-69028 HEIDELBERG,GERMANY

[2] EUROPEAN MOLEC BIOL LAB,PEPTIDE & PROT GRP,HEIDELBERG,GERMANY

[3] GERMAN CANC RES CTR,W-6900 HEIDELBERG,GERMANY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 223卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1994.tb19029.x

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：

Negative factor (Nef) protein from human immunodeficiency virus type 1 (HIV-1) is cleaved into two well-defined domains by the HIV-1-encoded protease. The cleavage site is located between Trp57 and Leu58 and is well conserved. The two domains are stable in the presence of protease for more than 48 h. The C-terminal core domain contains a well-conserved well-folded region. The cleavage releases the core domain from the myristoylated membrane anchor domain. As is the case for other HIV proteins, cleavage of Nef could be crucial for correct biological function.

引用

页码：589 / 593

页数：5

共 36 条

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