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M9480146.TXT
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1994-08-09
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Document 0146
DOCN M9480146
TI Identification of functional sites on bovine leukemia virus envelope
glycoproteins using structural and immunological data.
DT 9410
AU Callebaut I; Portetelle D; Burny A; Mornon JP; Departement des
Macromolecules Biologiques--Laboratoire de;
Mineralogie-Cristallographie, CNRS URA09, Universites Paris,; France.
SO Eur J Biochem. 1994 Jun 1;222(2):405-14. Unique Identifier : AIDSLINE
MED/94291634
AB Sequence analysis using the sensitive hydrophobic cluster analysis
method shows that the bovine leukemia virus envelope glycoproteins
conserve the general organization of the influenza hemagglutinin into a
'stem', containing the external part of the transmembrane glycoprotein
and the N-terminal and C-terminal parts of the external glycoprotein,
and a 'head', containing only external glycoprotein residues. However,
our analysis suggests, for the first time, that the bovine leukemia
virus envelope head will not adopt the typical 'jelly-roll' fold of the
influenza A hemagglutinin head, but most likely folds into another type
of 'Greek-key' structure corresponding to the overall topology of
constant immunoglobulin domains. We constructed a three-dimensional
model for the bovine leukemia virus envelope head by homology modeling
using the crystal structure of the human histocompatibility antigen
HLA-A2 alpha 3 domain. Furthermore, we propose a general model for the
oligomeric organization of this head, based on the hemagglutinin trimer.
The proposed structural organization of bovine leukemia virus external
glycoprotein is further supported by antipeptide and monoclonal antibody
reactivities. Our modeling study suggests that the loops of the two
neutralizing peptides located in the head are adjacent at the top of the
domain and define a potential interaction site of the external
glycoprotein with its cellular receptor. This site is topologically
similar to the binding site of hemagglutinin with its cellular receptor,
sialic acid. The other neutralizing peptides are located within a small
domain linking the head to the stem. These data are of interest for
defining other oncoviral glycoproteins heads and receptor-binding sites.
DE Amino Acid Sequence Comparative Study Glycoproteins/*CHEMISTRY Human
HLA-A2 Antigen/CHEMISTRY HTLV-I/CHEMISTRY Lentivirus/CHEMISTRY
Leukemia Virus, Bovine/*CHEMISTRY Models, Structural Molecular
Sequence Data Orthomyxoviruses Type A/CHEMISTRY *Protein Conformation
*Protein Structure, Secondary Retroviridae/*CHEMISTRY Sequence
Homology, Amino Acid Support, Non-U.S. Gov't Viral Envelope
Proteins/*CHEMISTRY JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).