1qy2

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spinqualitylabelsall models 1qy2, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Thermodynamics of Binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the Major Urinary Protein

Overview

In the present study we examine the thermodynamics of binding of two, related pyrazine-derived ligands to the major urinary protein, MUP-I, using a combination of isothermal titration calorimetry (ITC), X-ray, crystallography, and NMR backbone (15)N and methyl side-chain (2)H, relaxation measurements. Global thermodynamics data derived from ITC, indicate that binding is driven by favorable enthalpic contributions, rather than the classical entropy-driven hydrophobic effect. Unfavorable, entropic contributions from the protein backbone and side-chain residues, in the vicinity of the binding pocket are partially offset by favorable, entropic contributions at adjacent positions, suggesting a "conformational, relay" mechanism whereby increased rigidity of residues on ligand binding, are accompanied by increased conformational freedom of side chains in, adjacent positions. The principal driving force governing ligand affinity, and specificity can be attributed to solvent-driven enthalpic effects from, desolvation of the protein binding pocket.

About this Structure

1QY2 is a Single protein structure of sequence from Mus musculus with CD, NA and IPZ as ligands. Full crystallographic information is available from OCA.

Reference

Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein., Bingham RJ, Findlay JB, Hsieh SY, Kalverda AP, Kjellberg A, Perazzolo C, Phillips SE, Seshadri K, Trinh CH, Turnbull WB, Bodenhausen G, Homans SW, J Am Chem Soc. 2004 Feb 18;126(6):1675-81. PMID:14871097

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