Binding of Full-Length HIV-1 gp120 to CD4 Induces Structural Reorientation around the gp120 Core
Small-angle x-ray scattering data on the unliganded full-length fully glycosylated HIV-1 gp120, the soluble CD4 (domains 1-2) receptor and their complex in solution are presented. Ab initio structure restorations using these data provides the first look at the envelope shape for the unliganded and the complexed gp120 molecule. Fitting known crystal structures of the unliganded SIV and the complexed HIV gp120 core regions within our resultant shape constraints reveals movement of the V3 loop upon binding.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 914230
- Report Number(s):
- BNL-78798-2007-JA; BIOJAU; TRN: US200809%%105
- Journal Information:
- Biophys. J., Vol. 91; ISSN 0006-3495
- Country of Publication:
- United States
- Language:
- English
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