Figure: Crystal structures of PIE12/IQN17 (Q577R) (PDB: 6PSA) and PIE12/IQN17 (WT PDB:3L37).
Figure: Protein interaction analysis of Q577R mutation.
Figure: SPR equilibrium binding data (in triplicate) for interaction between immobilized IZN36 (WT or Q577R) and PIE12 monomer.
Figure: Stereoview of the overlay of crystal structures of PIE12 binding to the WT (yellow) and a mutant (Q577R, turquoise) pocket showing the disruption of hydrogen bonding interactions mediated by Q577.
Figure: The calculated K
Discussion: Efforts are underway to discover novel d-peptide entry inhibitors that maintain high affinity to both the native and Q577R pockets.
HIV-1 gp41 Residues Modulate CD4-Induced Conformational Changes in the Envelope Glycoprotein and Evolution of a Relaxed Conformation of gp120.
Abstract: While all Envs show increased neutralization sensitivity to mimetic CD4 (mCD4), Envs with either the E560K or Q577R HR1 mutation reduced conformational reactivity to CD4 that resisted viral inactivation and triggering to the 6HB.
HIV mutation literature information.
PMID: 
2019
Retrovirology
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