2ft9: Difference between revisions

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New page: left|200px<br /><applet load="2ft9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ft9, resolution 2.50Å" /> '''Crystal structure of...
 
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[[Image:2ft9.gif|left|200px]]<br /><applet load="2ft9" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2ft9.gif|left|200px]]<br /><applet load="2ft9" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2ft9, resolution 2.50&Aring;" />
caption="2ft9, resolution 2.50&Aring;" />
'''Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid'''<br />
'''Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid'''<br />


==Overview==
==Overview==
The family of the liver bile acid-binding proteins (L-BABPs), formerly, called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and, sequence similarity with the paralogous liver fatty acid-binding proteins, (L-FABPs) but has a different stoichiometry and specificity of ligand, binding. This article describes the first X-ray structure of a member of, the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two, different ligands: cholic and oleic acid. The protein binds one molecule, of oleic acid in a position that is significantly different from that of, either of the two molecules that bind to rat liver FABP. The stoichiometry, of binding of cholate is of two ligands per protein molecule, as observed, in chicken L-BABP. The cholate molecule that binds buried most deeply into, the internal cavity overlaps well with the analogous bound to chicken, L-BABP, whereas the second molecule, which interacts with the first only, through hydrophobic contacts, is more external and exposed to the solvent.
The family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent.


==About this Structure==
==About this Structure==
2FT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ambystoma_mexicanum Ambystoma mexicanum] with CHD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FT9 OCA].  
2FT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ambystoma_mexicanum Ambystoma mexicanum] with <scene name='pdbligand=CHD:'>CHD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FT9 OCA].  


==Reference==
==Reference==
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[[Category: Capaldi, S.]]
[[Category: Capaldi, S.]]
[[Category: Guariento, M.]]
[[Category: Guariento, M.]]
[[Category: Monaco, H.L.]]
[[Category: Monaco, H L.]]
[[Category: Perduca, M.]]
[[Category: Perduca, M.]]
[[Category: Pietro, S.M.Di.]]
[[Category: Pietro, S M.Di.]]
[[Category: Santome, J.A.]]
[[Category: Santome, J A.]]
[[Category: CHD]]
[[Category: CHD]]
[[Category: axolotl]]
[[Category: axolotl]]
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[[Category: liver bile acid-binding protein]]
[[Category: liver bile acid-binding protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:45:16 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:53 2008''

Revision as of 18:24, 21 February 2008

File:2ft9.gif


2ft9, resolution 2.50Å

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Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid

OverviewOverview

The family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent.

About this StructureAbout this Structure

2FT9 is a Single protein structure of sequence from Ambystoma mexicanum with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid., Capaldi S, Guariento M, Perduca M, Di Pietro SM, Santome JA, Monaco HL, Proteins. 2006 Jul 1;64(1):79-88. PMID:16555310

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