Binding of Full-Length HIV-1 gp120 to CD4 Induces Structural Reorientation around the gp120 Core
Abstract
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.
- Authors:
- Publication Date:
- Research Org.:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Org.:
- Doe - Office Of Science
- OSTI Identifier:
- 914230
- Report Number(s):
- BNL-78798-2007-JA
Journal ID: ISSN 0006-3495; BIOJAU; TRN: US200809%%105
- DOE Contract Number:
- DE-AC02-98CH10886
- Resource Type:
- Journal Article
- Journal Name:
- Biophys. J.
- Additional Journal Information:
- Journal Volume: 91; Journal ID: ISSN 0006-3495
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 36 MATERIALS SCIENCE; AIDS VIRUS; CRYSTAL STRUCTURE; SCATTERING; SHAPE; national synchrotron light source
Citation Formats
Ashish, F, Garg, R, Anguita, J, and Krueger, J. Binding of Full-Length HIV-1 gp120 to CD4 Induces Structural Reorientation around the gp120 Core. United States: N. p., 2006.
Web. doi:10.1529/biophysj.106.090381.
Ashish, F, Garg, R, Anguita, J, & Krueger, J. Binding of Full-Length HIV-1 gp120 to CD4 Induces Structural Reorientation around the gp120 Core. United States. https://doi.org/10.1529/biophysj.106.090381
Ashish, F, Garg, R, Anguita, J, and Krueger, J. 2006.
"Binding of Full-Length HIV-1 gp120 to CD4 Induces Structural Reorientation around the gp120 Core". United States. https://doi.org/10.1529/biophysj.106.090381.
@article{osti_914230,
title = {Binding of Full-Length HIV-1 gp120 to CD4 Induces Structural Reorientation around the gp120 Core},
author = {Ashish, F and Garg, R and Anguita, J and Krueger, J},
abstractNote = {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.},
doi = {10.1529/biophysj.106.090381},
url = {https://www.osti.gov/biblio/914230},
journal = {Biophys. J.},
issn = {0006-3495},
number = ,
volume = 91,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}
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