2ans

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2ans, resolution 2.5Å

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ADIPOCYTE LIPID BINDING PROTEIN COMPLEXED WITH 1-ANILINO-8-NAPHTHALENE SULFONATE

Overview

The fluorescent probe anilinonaphthalene-8-sulfonate binds to adipocyte, lipid binding protein at a site that competes with normal physiological, ligands, such as fatty acids. Binding to the protein is accompanied by a, relatively large increase in fluorescent intensity. To correlate the major, change in optical properties and to determine the mechanism of competitive, inhibition with fatty acids, the crystal structure of the protein with the, bound fluorophore has been determined. In addition, the thermodynamic, contributions to the binding reaction have been studied by titration, calorimetry. Because the binding site is in a relatively internal, position, kinetic studies have also been carried out to determine k(on)., The results indicate that binding is not accompanied by any major, conformational change. However, the negatively charged sulfonate moiety is, not positioned the same as the carboxylate of fatty acid ligands as, determined in previous studies. Nonetheless, the binding reaction is still, driven by enthalpic effects. As judged by the crystallographic structure, a significant amount of the surface of the fluorophore is no longer, exposed to water in the bound state.

About this Structure

2ANS is a Single protein structure of sequence from Mus musculus with CL and 2AN as ligands. Full crystallographic information is available from OCA.

Reference

Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate., Ory JJ, Banaszak LJ, Biophys J. 1999 Aug;77(2):1107-16. PMID:10423455

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