Opening dynamics of HIV-1 gp120 upon receptor binding is dictated by a key hydrophobic core
Author:
Affiliation:
1. Key Laboratory of System Biomedicine (Ministry of Education)
2. Shanghai Center for Systems Biomedicine
3. Shanghai Jiao Tong University
4. Shanghai 200240
5. China
Abstract
One hydrophobic core flanked by V1V2, V3 and β20 of HIV-1 gp120 is responsible for mediating the opening dynamics of gp120 upon receptor binding.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP04613E
Reference122 articles.
1. Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth
2. Delineating Antibody Recognition in Polyclonal Sera from Patterns of HIV-1 Isolate Neutralization
3. Affinity Maturation of a Potent Family of HIV Antibodies Is Primarily Focused on Accommodating or Avoiding Glycans
4. Minimally Mutated HIV-1 Broadly Neutralizing Antibodies to Guide Reductionist Vaccine Design
5. Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120
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