From owner-biophysics@net.bio.net Wed Jan 28 22:00:00 1998
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From: "Carol Gross"  <cgross@biosci.cbs.umn.edu>
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Subject: Annual Meeting - abstract addition
Date: 29 Jan 1998 07:30:18 -0800
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1998  BIOPHYSICAL SOCIETY ANNUAL MEETING

MEMBRANE STRUCTURE & ASSEMBLY SUBGROUP
Sunday, February 22,  12:30 - 5:30 p.m.. Room 1204A
Viral Fusion Proteins: Progress in Structure and Function

(12:30 p.m. Speaker abstract - not in abstract book)

COILED COILS AND MEMBRANE FUSION. Peter S. Kim, Whitehead Institute, 
Biomedical Research, Cambridge, MA 02142.

In order for an enveloped virus to infect cells, the membrane
surrounding the virus needs to fuse with the membrane surrounding
the cell.  Membrane fusion is regulated by the conformational state
of surface glycoproteins, that switch from the native
(non-fusogenic) structure to the fusogenic (fusion-active)
conformation.  Earlier studies revealed that, for the influenza
hemagglutinin protein, this conformational change utilizes a
"spring-loaded" mechanism in which the coiled-coil stem of the
native protein extends, relocating the hydrophobic fusion peptide,
by 100 Angstroms, toward the target membrane.  There is a striking
similarity between the influenza structure and the fusogenic
structures of the envelope proteins from murine leukemia virus and
human immunodeficiency virus type 1 (HIV-1).  The core structure of
gp41 from the HIV envelope protein, taken together with other
studies on the inhibitory properties of peptides derived from this
core, suggests avenues for the design/discovery of small molecule
inhibitors of HIV infection. 


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