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[[Image:1lib.gif|left|200px]]<br /><applet load="1lib" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lib, resolution 1.7&Aring;" />
'''THE ADIPOCYTE LIPID-BINDING PROTEIN AT 1.6 ANGSTROMS RESOLUTION: CRYSTAL STRUCTURES OF THE APOPROTEIN AND WITH BOUND SATURATED AND UNSATURATED FATTY ACIDS'''<br />


==Overview==
==THE ADIPOCYTE LIPID-BINDING PROTEIN AT 1.6 ANGSTROMS RESOLUTION: CRYSTAL STRUCTURES OF THE APOPROTEIN AND WITH BOUND SATURATED AND UNSATURATED FATTY ACIDS==
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.
<StructureSection load='1lib' size='340' side='right'caption='[[1lib]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lib]] is a 1 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=1LIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LIB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=1lib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lib OCA], [https://pdbe.org/1lib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lib RCSB], [https://www.ebi.ac.uk/pdbsum/1lib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lib ProSAT]</span></td></tr>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/li/1lib_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lib ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1LIB OCA].
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8463311 8463311]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Banaszak LJ]]
[[Category: Banaszak, L J.]]
[[Category: Bernlohr DA]]
[[Category: Bernlohr, D A.]]
[[Category: Zu Z]]
[[Category: Zu, Z.]]
[[Category: lipid-binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:13 2008''

Latest revision as of 10:33, 14 February 2024

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

Structural highlights

1lib is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
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.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

1lib, resolution 1.70Å

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