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Fig. 5 | Retrovirology

Fig. 5

From: Mutations of Glu560 within HIV-1 Envelope Glycoprotein N-terminal heptad repeat region contribute to resistance to peptide inhibitors of virus entry

Fig. 5

Modeling the mutations of Glutamic acid 560 (E560) in the six-helix bundle (6HB). The wild-type E560 and mutations E560K/D/G are modeled in the 6HB conformation (PDB code: 1AIK) in a ribbon model in longitudinal view. a E560 residue interacts with Q650 in C34 of inter-protomer gp41 via hydrogen bond which has 3.27 Å distances between two residues. b The mutation E560K changed into the positively charged residue and has longer side chain than wild type, and it still interacts with Q650 with shorter distance between them (2.37 Å), or probably it forms two hydrogen bonds with nitrogen atom of Q650. c E560D mutation has only shorter side chain than wild type and may interrupt the hydrogen bond with the longer distance (3.91 Å) between E560D and Q650. d E560G mutation removes the interaction between E560 and Q650. Interatomic distances are marked by the dashed lines

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Retrovirology

ISSN: 1742-4690

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