1mvg: Difference between revisions

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[[Image:1mvg.gif|left|200px]]
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{{STRUCTURE_1mvg|  PDB=1mvg  |  SCENE=  }}
'''NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)'''


==NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)==
<StructureSection load='1mvg' size='340' side='right'caption='[[1mvg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mvg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1mvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvg OCA], [https://pdbe.org/1mvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvg RCSB], [https://www.ebi.ac.uk/pdbsum/1mvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABPL_CHICK FABPL_CHICK] 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. Binds 2 molecules of cholate per subunit.
== 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/mv/1mvg_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=1mvg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by (1)H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel beta-strands organised in two nearly ortogonal beta-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.


==Overview==
Solution structure of chicken liver basic fatty acid binding protein.,Vasile F, Ragona L, Catalano M, Zetta L, Perduca M, Monaco H, Molinari H J Biomol NMR. 2003 Feb;25(2):157-60. PMID:12652125<ref>PMID:12652125</ref>
Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by (1)H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel beta-strands organised in two nearly ortogonal beta-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1MVG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVG OCA].
</div>
<div class="pdbe-citations 1mvg" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solution structure of chicken liver basic fatty acid binding protein., Vasile F, Ragona L, Catalano M, Zetta L, Perduca M, Monaco H, Molinari H, J Biomol NMR. 2003 Feb;25(2):157-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12652125 12652125]
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Catalano, M.]]
[[Category: Catalano M]]
[[Category: Molinari, H.]]
[[Category: Molinari H]]
[[Category: Monaco, H.]]
[[Category: Monaco H]]
[[Category: Perduca, M.]]
[[Category: Perduca M]]
[[Category: Ragona, L.]]
[[Category: Ragona L]]
[[Category: Vasile, F.]]
[[Category: Vasile F]]
[[Category: Zetta, L.]]
[[Category: Zetta L]]
[[Category: Beta-barrel]]
[[Category: Calycin]]
[[Category: Fatty acid binding protein]]
[[Category: Helix-turn-helix motif]]
[[Category: Ten antiparallel beta strand]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:45:59 2008''

Latest revision as of 11:51, 22 May 2024

NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)

Structural highlights

1mvg is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABPL_CHICK 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. Binds 2 molecules of cholate per subunit.

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

Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by (1)H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel beta-strands organised in two nearly ortogonal beta-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.

Solution structure of chicken liver basic fatty acid binding protein.,Vasile F, Ragona L, Catalano M, Zetta L, Perduca M, Monaco H, Molinari H J Biomol NMR. 2003 Feb;25(2):157-60. PMID:12652125[1]

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

See Also

References

  1. Vasile F, Ragona L, Catalano M, Zetta L, Perduca M, Monaco H, Molinari H. Solution structure of chicken liver basic fatty acid binding protein. J Biomol NMR. 2003 Feb;25(2):157-60. PMID:12652125
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