home
***
CD-ROM
|
disk
|
FTP
|
other
***
search
/
The Arsenal Files 6
/
The Arsenal Files 6 (Arsenal Computer).ISO
/
health
/
med9603.zip
/
M9630333.TXT
< prev
next >
Wrap
Text File
|
1996-02-27
|
3KB
|
51 lines
Document 0333
DOCN M9630333
TI First glimpses at structure-function relationships of the nucleocapsid
protein of retroviruses.
DT 9603
AU Darlix JL; Lapadat-Tapolsky M; de Rocquigny H; Roques BP; LaboRetro,
Unite de Virologie humaine INSERM U412, Ecole Normale; Superieure de
Lyon, France.
SO J Mol Biol. 1995 Dec 8;254(4):523-37. Unique Identifier : AIDSLINE
MED/96102278
AB Retroviruses are a family of widespread small animal viruses about 110
nm in diameter, composed of an inner core surrounded by an outer
envelope formed of a lipid bilayer of cellular origin in which are
anchored viral glycoproteins. The inner core is formed by an outer shell
of capsid protein molecules (CA protein) surrounding the dimeric RNA
genome in close association with about 2000 molecules of nucleocapsid
protein (NC protein) and molecules of reverse transcriptase (RT) and
integrase (IN). Conversion of the genomic single-stranded RNA into a
double-stranded proviral DNA by RT takes place in the nucleocapsid
substructure and involves two DNA strand transfers to generate the long
terminal repeats (LTR) required for IN-mediated integration of the
proviral DNA into the cellular genome and its expression. In this review
we have summarized some of the properties and functions of the
nucleocapsid protein of the most intensely studied oncoretroviruses
(MuLV and ASLV) and lentiviruses (HIV-1). Recent biochemical and genetic
data on retroviral NC proteins have shown that this small viral protein
endowed with a strong affinity for nucleic acids exhibits nucleic acid
annealing and strand transfer activities and is required for the
formation of infectious viral particles. These new activities of NC
protein are most probably necessary at the early steps of proviral DNA
synthesis. The 3-D structures of HIV-1 and MoMuLV NC proteins, deduced
from NMR studies, are characterized by a central globular domain with
one (MoMuLV) or two (HIV-1) zinc fingers. This should facilitate a
rational approach of new anti-HIV therapies based on inhibition of NC
protein functions. Due to space limitations and the very abundant
literature on retroviruses, references to articles prior to the
publication of the second volume of RNA Tumor Viruses in 1985 (Weiss et
al., 1985) will be minimal. We also direct the reader to an excellent
review which summarizes recent insights into biochemical and structural
aspects of the retroviral enzymes PR, RT and IN (Katz & Skalka, 1994).
DE Amino Acid Sequence Capsid/*CHEMISTRY/METABOLISM/*PHYSIOLOGY Models,
Molecular Molecular Sequence Data Nucleic Acids/METABOLISM
Retroviridae/*CHEMISTRY RNA, Transfer RNA, Viral Structure-Activity
Relationship Support, Non-U.S. Gov't Transcription, Genetic Viral
Core Proteins/*CHEMISTRY/METABOLISM/*PHYSIOLOGY JOURNAL ARTICLE REVIEW
REVIEW, TUTORIAL
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).