scholarly journals Probing intrinsic dynamics and conformational transition of HIV gp120 by molecular dynamics simulation

RSC Advances ◽  
2020 ◽  
Vol 10 (51) ◽  
pp. 30499-30507
Author(s):  
Yi Li ◽  
Xiao-Ling Zhang ◽  
Xue Yuan ◽  
Jiang-Chun Hou ◽  
Peng Sang ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Viral Infection ◽  
Envelope Glycoprotein ◽  
Immune Escape ◽  
Conformational Transition ◽  
Dynamics Simulation ◽  
Glycoprotein Gp120 ◽  
Hiv Gp120 ◽  
Hiv Envelope

The HIV envelope glycoprotein gp120 has evolved two distinct conformational states to balance viral infection and immune escape.

scholarly journals Correction: Probing intrinsic dynamics and conformational transition of HIV gp120 by molecular dynamics simulation

RSC Advances ◽  
2020 ◽  
Vol 10 (61) ◽  
pp. 36988-36988
Author(s):  
Yi Li ◽  
Xiao-Ling Zhang ◽  
Xue Yuan ◽  
Jiang-Chun Hou ◽  
Peng Sang ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Conformational Transition ◽  
Dynamics Simulation ◽  
Hiv Gp120

Correction for ‘Probing intrinsic dynamics and conformational transition of HIV gp120 by molecular dynamics simulation’ by Yi Li et al., RSC Adv., 2020, 10, 30499–30507, DOI: 10.1039/d0ra06416e.

scholarly journals Probing the HIV gp120 Envelope Glycoprotein Conformation by NMR

2011 ◽  
Vol 286 (27) ◽  
pp. 23975-23981 ◽  
Author(s):  
Jessica Celigoy ◽  
Benjamin Ramirez ◽  
Lin Tao ◽  
Lijun Rong ◽  
Lianying Yan ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Structural Information ◽  
Close Contact ◽  
Critical Role ◽  
Binding Mode ◽  
Subtle Difference ◽  
Glycoprotein Gp120 ◽  
Hiv Gp120 ◽  
Hiv Envelope ◽  
Gp120 Structure

The HIV envelope glycoprotein gp120 plays a critical role in virus entry, and thus, its structure is of extreme interest for the development of novel therapeutics and vaccines. To date, high resolution structural information about gp120 in complex with gp41 has proven intractable. In this study, we characterize the structural properties of gp120 in the presence and absence of gp41 domains by NMR. Using the peptide probe 12p1 (sequence, RINNIPWSEAMM), which was identified previously as an entry inhibitor that binds to gp120, we identify atoms of 12p1 in close contact with gp120 in the monomeric and trimeric states. Interestingly, the binding mode of 12p1 with gp120 is similar for clades B and C. In addition, we show a subtle difference in the binding mode of 12p1 in the presence of gp41 domains, i.e. the trimeric state, which we interpret as small differences in the gp120 structure in the presence of gp41.

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