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. 2012 Aug 30;8(8):e1002896. doi: 10.1371/journal.ppat.1002896

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Isothermal titration calorimetry (ITC) of CPSF6_313–327 against CA^N domains of lentiviral capsids. CPSF6_313–327 binding to HIV-1 is specific (A), being abolished by CA mutation N74D (B). CPSF6_313–327 also binds to diverse primate lentiviral capsids, HIV-2, FIV and SIVmac (C). The stoichiometry (N), affinity (K_d), enthalpy (ΔH) and entropy (ΔS) of interaction are shown.