Abstract:
:HIV gp120 is specifically cleaved at a single site in the V3 loop between Arg315 and Ala316 by thrombin. Previous observations by others have indicated that binding to CD4 enhances the rate of V3 loop cleavage, and that this cleavage is a prerequisite for HIV infection. Other observations also suggest that the cleavage site is in a type II beta-turn centered at Pro313-Gly314. However, our docking experiments indicate that this conformation cannot dock to thrombin and other trypsin-like serine proteases. Thus, based on the thrombin-bound conformation of peptide substrates, we propose that CD4 binding, at a site remote from the V3 loop, induces and stabilizes a trans to cis isomerization of the highly conserved residue Pro313, and that this conformational shift is a prerequisite for cleavage by a 'thrombin-like' cellular protease and subsequent infection.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Johnson ME,Lin Z,Padmanabhan K,Tulinsky A,Kahn Mdoi
10.1016/0014-5793(94)80618-7subject
Has Abstractpub_date
1994-01-03 00:00:00pages
4-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(94)80618-7journal_volume
337pub_type
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