Abstract：
:A 15-residue fragment within the major continuous domain of gp120 from HIV-1 that can bind independently to the CD4 receptor has been shown to have the property of behaving as a solvent polarity-dependent conformational switch. The switch behavior (cooperative transition from beta-sheet to helical conformation as a function of solvent polarity), which is conserved among strains with the widest sequence variability possible, appears to be a prerequisite for the CD4-binding ability. A number of switch inhibitors have been identified that destroy the conformational switch in the 15-residue fragment and concurrently its ability to bind to CD4-expressing cells. It can now be shown that the switch behavior and its inhibition by substances with certain shared structural characteristics are not restricted to the 15-residue subfragment, but are reflected by the behavior of the entire 44-residue binding domain. Further, substances active as switch inhibitors have an immediate effect on the conformation of the 44-residue fragment in aqueous buffer whereas inactive substances do not. The predictive value of this as a screening method is demonstrated in testing a number of new potential switch inhibitory compounds.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Graf von Stosch A,Kinzel V,Reed Jdoi
10.1021/bi952045wsubject
Has Abstractpub_date
1996-01-16 00:00:00pages
411-7issue
2eissn
0006-2960issn
1520-4995pii
bi952045wjournal_volume
35pub_type
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