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. Author manuscript; available in PMC: 2013 Feb 9.
Published in final edited form as: J Med Chem. 2011 Dec 2;55(3):977–994. doi: 10.1021/jm200568c

Figure 4.

Figure 4

A hypothetic mechanism for how CXCR4 exploits the flexible ligand binding surface of CXCR4 to evade the recognition of a neutralizing antibody while retaining the ability to bind CXCR4 for cellular entry. The flexibility of the CXCR4–ligand interface may allow sequence and conformational variations of V3 loop of the HIV-1 gp120. If the resulting changes in the gp120 V3 loop are accommodated by the flexible binding surface of CXCR4 but not by that of an antibody, the virus can then evade neutralizing antibodies while maintaining a high affinity for the coreceptor that is necessary for viral entry into the cell.