Mutation in the D1 domain of CD4 receptor modulates the binding affinity to HIV-1 gp120.

ABSTRACT: The gp120 surface subunit of HIV-1 envelope lycoprotein (Env) is the key component for the viral entry process through interaction with the CD4 binding site (CD4bs) of the primary receptor CD4. The point mutant was introduced into SD1, a CD4 D1 variant, to enhance the interaction with HIV-1 gp120.The three-dimensional structures of gp120 and SD1 were determined using homology modeling based on the results previously determined by X-ray crystallography. The binding models were carried out via protein-protein docking tools. The 5 best docking solutions were retained according to the docking scores and were used for structural assessment. Our results demonstrated the consistency between the 3D models of gp120 and SD1 predicted by molecular docking calculations and the co-crystallized d

SUBMITTER: Shao J 

PROVIDER: S-EPMC9832346 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature