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1996-02-26
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Document 0983
DOCN M9620983
TI A trimeric subdomain of the simian immunodeficiency virus envelope
glycoprotein.
DT 9602
AU Blacklow SC; Lu M; Kim PS; Howard Hughes Medical Institute, Whitehead
Institute for; Biomedical Research, Department of Biology,
Massachusetts; Institute of Technology, Cambridge 02142, USA.
SO Biochemistry. 1995 Nov 21;34(46):14955-62. Unique Identifier : AIDSLINE
MED/96072732
AB Previous attempts to define the oligomeric state of the HIV and SIV
envelope glycoproteins have yielded conflicting results. We have
produced in Escherichia coli a recombinant model for the ectodomain of
the SIV envelope protein gp41 and have identified a small, trimeric
subdomain by proteolytic digestion of this gp41 fragment. The subdomain
assembles from two peptide fragments, spanning residues 28-80 (N28-80)
and residues 107-149 (C107-149) of SIV gp41. Each of these peptides
contains a 4,3-hydrophobic repeat, the hallmark of coiled-coil
sequences. Upon mixing, the peptides form a highly helical, trimeric
complex [3(N+C)] that resists proteolysis and has a melting temperature
(Tm) above 90 degrees C in physiological buffer. The N- and C-terminal
fragments are antiparallel to each other in the complex, as judged by
the observation that digestion of a variant recombinant protein
truncated at the amino terminus yields a C-terminal fragment shortened
at its carboxy terminus. The N28-80 peptide contains more positions
within the heptad repeat than C107-149 that are predominantly
hydrophobic, suggesting that N28-80 is buried in the interior of the
complex. We propose that the complex consists of a parallel, trimeric
coiled-coil of the N-terminal peptide, encircled by three C-terminal
peptide helices arranged in an antiparallel fashion, and that this
complex forms a core within the gp41 extracellular domain.
DE Amino Acid Sequence Chromatography, High Pressure Liquid Circular
Dichroism Comparative Study Heat Hydrogen-Ion Concentration
HIV/CHEMISTRY Macromolecular Systems Membrane Glycoproteins/*CHEMISTRY
Molecular Sequence Data Peptide Fragments/CHEMISTRY/METABOLISM Protein
Folding Protein Structure, Secondary Recombinant Proteins/CHEMISTRY
Retroviridae Proteins/*CHEMISTRY Serine Proteinases/METABOLISM
Support, Non-U.S. Gov't SIV/*CHEMISTRY 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).