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| | <StructureSection load='2ans' size='340' side='right'caption='[[2ans]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2ans' size='340' side='right'caption='[[2ans]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ans]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ans]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2AN:8-ANILINO-1-NAPHTHALENE+SULFONATE'>2AN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ans FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ans OCA], [http://pdbe.org/2ans PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ans RCSB], [http://www.ebi.ac.uk/pdbsum/2ans PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ans ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AN:8-ANILINO-1-NAPHTHALENE+SULFONATE'>2AN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ans FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ans OCA], [https://pdbe.org/2ans PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ans RCSB], [https://www.ebi.ac.uk/pdbsum/2ans PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ans ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FABP4_MOUSE FABP4_MOUSE]] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.<ref>PMID:12077340</ref> <ref>PMID:16574478</ref> <ref>PMID:17516629</ref> | + | [https://www.uniprot.org/uniprot/FABP4_MOUSE FABP4_MOUSE] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.<ref>PMID:12077340</ref> <ref>PMID:16574478</ref> <ref>PMID:17516629</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Banaszak, L J]] | + | [[Category: Banaszak LJ]] |
| - | [[Category: Ory, J J]] | + | [[Category: Ory JJ]] |
| - | [[Category: Fluorescent probe]]
| + | |
| - | [[Category: Lipid binding protein]]
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| - | [[Category: Lipid-binding protein]]
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| Structural highlights
Function
FABP4_MOUSE Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tan NS, Shaw NS, Vinckenbosch N, Liu P, Yasmin R, Desvergne B, Wahli W, Noy N. Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription. Mol Cell Biol. 2002 Jul;22(14):5114-27. PMID:12077340
- ↑ Adida A, Spener F. Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor gamma agonists in cultured cell. Biochim Biophys Acta. 2006 Feb;1761(2):172-81. Epub 2006 Mar 9. PMID:16574478 doi:http://dx.doi.org/S1388-1981(06)00031-X
- ↑ Ayers SD, Nedrow KL, Gillilan RE, Noy N. Continuous nucleocytoplasmic shuttling underlies transcriptional activation of PPARgamma by FABP4. Biochemistry. 2007 Jun 12;46(23):6744-52. Epub 2007 May 22. PMID:17516629 doi:http://dx.doi.org/10.1021/bi700047a
- ↑ Ory JJ, Banaszak LJ. Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1, 8-anilinonaphthalene-8-sulfonate. Biophys J. 1999 Aug;77(2):1107-16. PMID:10423455
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