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Comment
. 2013 Jun 4;21(6):871-2.
doi: 10.1016/j.str.2013.05.004.

Blocking HIV-1 gp120 at the Phe43 cavity: if the extension fits…

Barna Dey  1 , Edward A Berger
Affiliations
Comment

Blocking HIV-1 gp120 at the Phe43 cavity: if the extension fits…

Barna Dey et al. Structure. .

Abstract

The Phe43 cavity is a mysterious feature in crystallographic structures of HIV-1 gp120-CD4 complexes. In this issue of Structure, Acharya and colleagues provide structural explanations for the potent neutralization by CD4 mimetic miniproteins with chemical extensions that fit into this cavity.

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Figures

Figure 1
Figure 1. The Phe43 cavity
CD4 (pink; only domain 1 is shown) binding induces formation of a ~150 Å3 interfacial pocket at the nexus of the gp120 inner domain (pale blue), outer domain (marine blue) and bridging sheet (purple); the phenyl ring of the Phe43 side chain (red) forms a lid to the cavity, and is the only contributing component from CD4. Generated using MacPyMOL from PDB 1RZK (Huang et al, 2004).
See this image and copyright information in PMC

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