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[[Image:1tw4.gif|left|200px]]


{{Structure
==Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid==
|PDB= 1tw4 |SIZE=350|CAPTION= <scene name='initialview01'>1tw4</scene>, resolution 2.00&Aring;
<StructureSection load='1tw4' size='340' side='right'caption='[[1tw4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CHD:CHOLIC ACID'>CHD</scene>
<table><tr><td colspan='2'>[[1tw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TW4 FirstGlance]. <br>
|ACTIVITY=  
</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&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</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=1tw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tw4 OCA], [https://pdbe.org/1tw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tw4 RCSB], [https://www.ebi.ac.uk/pdbsum/1tw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tw4 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/tw/1tw4_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=1tw4 ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid'''
==See Also==
 
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Two paralogous groups of liver fatty acid-binding proteins (FABPs) have been described: the mammalian type liver FABPs and the basic type (Lb-FABPs) characterized in several vertebrates but not in mammals. The two groups have similar sequences and share a highly conserved three-dimensional structure, but their specificity and stoichiometry of binding are different. The crystal structure of chicken Lb-FABP complexed with cholic acid and that of the apoprotein refined to 2.0 A resolution are presented in this paper. The two forms of the protein crystallize in different space groups, and significant changes are observed between the two conformations. The holoprotein binds two molecules of cholate in the interior cavity, and the contacts observed between the two ligands can help to explain the reason for this stoichiometry of binding. Most of the amino acids involved in ligand binding are conserved in other members of the Lb-FABP family. Since the amino acid sequence of the Lb-FABPs is more similar to that of the bile acid-binding proteins than to that of the L-FABPs, the possibility that the Lb-FABPs might be more appropriately called liver bile acid-binding proteins (L-BABPs) is suggested.
 
==About this Structure==
1TW4 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=1TW4 OCA].
 
==Reference==
Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid., Nichesola D, Perduca M, Capaldi S, Carrizo ME, Righetti PG, Monaco HL, Biochemistry. 2004 Nov 9;43(44):14072-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15518556 15518556]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Capaldi, S.]]
[[Category: Capaldi S]]
[[Category: Carrizo, M E.]]
[[Category: Carrizo ME]]
[[Category: Monaco, H L.]]
[[Category: Monaco HL]]
[[Category: Nichesola, D.]]
[[Category: Nichesola D]]
[[Category: Perduca, M.]]
[[Category: Perduca M]]
[[Category: Righetti, P G.]]
[[Category: Righetti PG]]
[[Category: CHD]]
[[Category: babp]]
[[Category: bile acid]]
[[Category: cholic acid]]
[[Category: fabp]]
[[Category: intracellular bile acid-binding protein]]
[[Category: lb-fabp]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:24:00 2008''

Latest revision as of 16:30, 13 March 2024

Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic AcidCrystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid

Structural highlights

1tw4 is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
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.

See Also

1tw4, resolution 2.00Å

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