Correlated mutations at gp120 positions 322 and 440: Implications for gp120 structure
Copyright policy )Correlated mutations at gp120 positions 322 and 440: Implications for gp120 structure
AbstractAnalysis of V3 and C4 sequences of HIV‐1 reveals correlated mutations at gp120 positions 322 and 440, and a very strong preference for a positively charged residue at position 440 when position 322 is negatively charged. This observation suggests that these two residues are close to each other and interact electrostatically in R5 viruses. This interaction was used to model V3 in the context of gp120 using NMR data for the V3 loop and the crystal structure of the gp120‐core. The interaction between residues 322 and 440 may serve as part of the molecular switch for HIV‐1 phenotype conversion. Proteins 2008. © 2008 Wiley‐Liss, Inc.
- Stanford University United States
- Weizmann Institute of Science Israel
Phenotype, Amino Acid Substitution, Databases, Genetic, Mutation, Static Electricity, HIV-1, HIV Envelope Protein gp120, Protein Structure, Secondary
Phenotype, Amino Acid Substitution, Databases, Genetic, Mutation, Static Electricity, HIV-1, HIV Envelope Protein gp120, Protein Structure, Secondary
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