Restraining the conformation of HIV-1 gp120 by removing a flexible loop.
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ABSTRACT:
SUBMITTER: Rits-Volloch S
PROVIDER: S-EPMC1618118 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Publications
Restraining the conformation of HIV-1 gp120 by removing a flexible loop.
Rits-Volloch Sophia S Frey Gary G Harrison Stephen C SC Chen Bing B
The EMBO journal 20060928 20
The trimeric HIV/SIV envelope glycoprotein, gp160, is cleaved to noncovalently associated fragments, gp120 and gp41. Binding of gp120 to viral receptors leads to large structural rearrangements in both fragments. The unliganded gp120 core has a disordered beta3-beta5 loop, which reconfigures upon CD4 binding into an ordered, extended strand. Molecular modeling suggests that residues in this loop may contact gp41. We show here that deletions in the beta3-beta5 loop of HIV-1 gp120 weaken the bindi ...[more]
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