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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).
-
-