1lfo

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{{Seed}}
 
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[[Image:1lfo.png|left|200px]]
 
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==LIVER FATTY ACID BINDING PROTEIN-OLEATE COMPLEX==
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The line below this paragraph, containing "STRUCTURE_1lfo", creates the "Structure Box" on the page.
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<StructureSection load='1lfo' size='340' side='right'caption='[[1lfo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1lfo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LFO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=BEO:BUTENOIC+ACID'>BEO</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
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{{STRUCTURE_1lfo| PDB=1lfo | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfo OCA], [https://pdbe.org/1lfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lfo RCSB], [https://www.ebi.ac.uk/pdbsum/1lfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABPL_RAT FABPL_RAT] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lf/1lfo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1lfo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the recombinant form of rat liver fatty acid-binding protein was completed to 2.3 A and refined to an R factor of 19.0%. The structural solution was obtained by molecular replacement using superimposed polyalanine coordinates of six intracellular lipid-binding proteins as a search probe. The entire amino acid sequence of rat liver fatty acid-binding protein along with an amino-terminal formyl-methionine was modeled in the crystal structure. In addition, the crystal was obtained in the presence of oleic acid, and the initial electron density clearly showed two fatty acid molecules bound within a central cavity. The carboxylate of one fatty acid molecule interacts with arginine 122 and is shielded from free solvent. It has an overall bent conformation. The more solvent-exposed carboxylate of the other oleate is located near the helix-turn-helix that caps one end of the beta-barrel, while the acyl chain lies in the interior. The cavity contains both polar and nonpolar residues but also shows extensive hydrophobic character around the nonpolar atoms of the ligands. The primary and secondary oleate binding sites appear to be totally interdependent, mainly because favorable hydrophobic interactions form between both aliphatic chains.
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===LIVER FATTY ACID BINDING PROTEIN-OLEATE COMPLEX===
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The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates.,Thompson J, Winter N, Terwey D, Bratt J, Banaszak L J Biol Chem. 1997 Mar 14;272(11):7140-50. PMID:9054409<ref>PMID:9054409</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1lfo" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9054409}}, adds the Publication Abstract to the page
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*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9054409 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9054409}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1LFO is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFO OCA].
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==Reference==
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<ref group="xtra">PMID:9054409</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Banaszak, L.]]
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[[Category: Banaszak L]]
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[[Category: Bratt, J.]]
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[[Category: Bratt J]]
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[[Category: Terwey, D.]]
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[[Category: Terwey D]]
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[[Category: Thompson, J.]]
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[[Category: Thompson J]]
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[[Category: Winter, N.]]
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[[Category: Winter N]]
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[[Category: Fatty acid binding protein]]
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[[Category: Intracellular lipid transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 10:27:08 2009''
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Current revision

LIVER FATTY ACID BINDING PROTEIN-OLEATE COMPLEX

PDB ID 1lfo

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