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• W2122306218 abstract "Inositol 1,4,5-trisphosphate (IP₃) receptors (IP₃R) are intracellular Ca²⁺ channels. Their opening is initiated by binding of IP₃ to the IP₃-binding core (IBC; residues 224–604 of IP₃R1) and transmitted to the pore via the suppressor domain (SD; residues 1–223). The major conformational changes leading to IP₃R activation occur within the N terminus (NT; residues 1–604). We therefore developed a high-throughput fluorescence polarization (FP) assay using a newly synthesized analog of IP₃, fluorescein isothiocyanate (FITC)-IP₃, to examine the thermodynamics of IP₃ and adenophostin A binding to the NT and IBC. Using both single-channel recording and the FP assay, we demonstrate that FITC-IP₃ is a high-affinity partial agonist of the IP₃R. Conventional [³H]IP₃ and FP assays provide similar estimates of the <i>K</i>_D for both IP₃ and adenophostin A in cytosol-like medium at 4°C. They further establish that the isolated IBC retains the ability of full-length IP₃R to bind adenophostin A with ∼10-fold greater affinity than IP₃. By examining the reversible effects of temperature on ligand binding, we established that favorable entropy changes (<i>T</i>Δ<i>S</i>) account for the greater affinities of both ligands for the IBC relative to the NT and for the greater affinity of adenophostin A relative to IP₃. The two agonists differ more substantially in the relative contribution of Δ<i>H</i> and <i>T</i>Δ<i>S</i> to binding to the IBC relative to the NT. This suggests that different initial binding events drive the IP₃R on convergent pathways toward a similar open state." @default.
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• W2122306218 date "2010-03-09" @default.
• W2122306218 modified "2023-09-28" @default.
• W2122306218 title "Binding of Inositol 1,4,5-trisphosphate (IP₃) and Adenophostin A to the N-Terminal region of the IP₃Receptor: Thermodynamic Analysis Using Fluorescence Polarization with a Novel IP₃Receptor Ligand" @default.
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• W2122306218 doi "https://doi.org/10.1124/mol.109.062596" @default.
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