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1lid

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Revision as of 10:46, 19 May 2021

THE ADIPOCYTE LIPID-BINDING PROTEIN AT 1.6 ANGSTROMS RESOLUTION: CRYSTAL STRUCTURES OF THE APOPROTEIN AND WITH BOUND SATURATED AND UNSATURATED FATTY ACIDS

Structural highlights

1lid is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Crystals of the adipocyte lipid-binding protein which diffract to near atomic resolution have been obtained in Na/K phosphate buffer/precipitant system. The structures of the apo-form and the protein with bound oleic acid and stearic acid have been determined and refined to 1.6-A resolution with R-factor around 18%. The conformations of the bound fatty acids are nearly the same. In both cases, the carboxylate group of the ligand interacts directly with Arg126 and Tyr128, indirectly with Arg106 through a water molecule. The hydrocarbon tail sticks out of the protein surface through a hydrophobic patch. Saturated and unsaturated fatty acids bind in essentially the same conformation. The remaining space of the binding pocket is filled with well ordered water molecules interacting with most of the polar side chains. Comparisons between the holo- and apostructures reveal that the hydrophobic patch on the protein surface formed by a helix and several tight turns might serve as a portal for lipid binding. Since the adipocyte lipid-binding protein is phosphorylated at Tyr19 by the insulin receptor kinase, the position of this side chain has been re-evaluated using the coordinates of the holo-forms. It appears that the position of Tyr19 does not change significantly upon the binding of either of the fatty acids.

The adipocyte lipid-binding protein at 1.6-A resolution. Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids.,Xu Z, Bernlohr DA, Banaszak LJ J Biol Chem. 1993 Apr 15;268(11):7874-84. PMID:8463311^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Xu Z, Bernlohr DA, Banaszak LJ. The adipocyte lipid-binding protein at 1.6-A resolution. Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids. J Biol Chem. 1993 Apr 15;268(11):7874-84. PMID:8463311

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lid"

@@ Line 3: / Line 3: @@
 <StructureSection load='1lid' size='340' side='right'caption='[[1lid]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lid]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LID FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LID FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></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=1lid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lid OCA], [http://pdbe.org/1lid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lid RCSB], [http://www.ebi.ac.uk/pdbsum/1lid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lid ProSAT]</span></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=1lid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lid OCA], [https://pdbe.org/1lid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lid RCSB], [https://www.ebi.ac.uk/pdbsum/1lid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lid ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1lid

From Proteopedia

Revision as of 10:46, 19 May 2021

THE ADIPOCYTE LIPID-BINDING PROTEIN AT 1.6 ANGSTROMS RESOLUTION: CRYSTAL STRUCTURES OF THE APOPROTEIN AND WITH BOUND SATURATED AND UNSATURATED FATTY ACIDS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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