1qy0
From Proteopedia
(New page: 200px<br /><applet load="1qy0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qy0, resolution 1.8Å" /> '''Thermodynamics of Bin...) |
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| - | [[Image:1qy0.gif|left|200px]]<br /><applet load="1qy0" size=" | + | [[Image:1qy0.gif|left|200px]]<br /><applet load="1qy0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qy0, resolution 1.8Å" /> | caption="1qy0, resolution 1.8Å" /> | ||
'''Thermodynamics of Binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the Major Urinary Protein'''<br /> | '''Thermodynamics of Binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the Major Urinary Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the present study we examine the thermodynamics of binding of two | + | 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== | ==About this Structure== | ||
| - | 1QY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CD, NA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bingham, R | + | [[Category: Bingham, R J.]] |
[[Category: Bodenhausen, G.]] | [[Category: Bodenhausen, G.]] | ||
| - | [[Category: Findlay, J | + | [[Category: Findlay, J B.C.]] |
| - | [[Category: Homans, S | + | [[Category: Homans, S W.]] |
| - | [[Category: Hsieh, S | + | [[Category: Hsieh, S Y.]] |
| - | [[Category: Kalverda, A | + | [[Category: Kalverda, A P.]] |
[[Category: Kjellberg, A.]] | [[Category: Kjellberg, A.]] | ||
[[Category: Perazzolo, C.]] | [[Category: Perazzolo, C.]] | ||
| - | [[Category: Phillips, S | + | [[Category: Phillips, S E.V.]] |
[[Category: Seshadri, K.]] | [[Category: Seshadri, K.]] | ||
| - | [[Category: Trinh, C | + | [[Category: Trinh, C H.]] |
| - | [[Category: Turnbull, W | + | [[Category: Turnbull, W B.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: lipocalin]] | [[Category: lipocalin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:55 2008'' |
Revision as of 12:44, 21 February 2008
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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
1QY0 is a Single protein structure of sequence from Mus musculus with , and 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
Page seeded by OCA on Thu Feb 21 14:44:55 2008
Categories: Mus musculus | Single protein | Bingham, R J. | Bodenhausen, G. | Findlay, J B.C. | Homans, S W. | Hsieh, S Y. | Kalverda, A P. | Kjellberg, A. | Perazzolo, C. | Phillips, S E.V. | Seshadri, K. | Trinh, C H. | Turnbull, W B. | CD | GOL | NA | Beta-barrel | Lipocalin
