2ans

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(New page: 200px<br /><applet load="2ans" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ans, resolution 2.5&Aring;" /> '''ADIPOCYTE LIPID BINDI...)
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[[Image:2ans.jpg|left|200px]]<br /><applet load="2ans" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ans, resolution 2.5&Aring;" />
caption="2ans, resolution 2.5&Aring;" />
'''ADIPOCYTE LIPID BINDING PROTEIN COMPLEXED WITH 1-ANILINO-8-NAPHTHALENE SULFONATE'''<br />
'''ADIPOCYTE LIPID BINDING PROTEIN COMPLEXED WITH 1-ANILINO-8-NAPHTHALENE SULFONATE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2ANS 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 CL and 2AN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ANS OCA].
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2ANS 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=CL:'>CL</scene> and <scene name='pdbligand=2AN:'>2AN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANS OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Banaszak, L.J.]]
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[[Category: Banaszak, L J.]]
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[[Category: Ory, J.J.]]
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[[Category: Ory, J J.]]
[[Category: 2AN]]
[[Category: 2AN]]
[[Category: CL]]
[[Category: CL]]
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[[Category: lipid-binding protein]]
[[Category: lipid-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:15:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:29:13 2008''

Revision as of 14:29, 21 February 2008


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 and 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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