2ft9: Difference between revisions

Revision as of 09:46, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ft9.png

Template:STRUCTURE 2ft9

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

Template:ABSTRACT PUBMED 16555310

About this StructureAbout this Structure

2FT9 is a Single protein structure of sequence from Ambystoma mexicanum. 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

Crystallization and preliminary X-ray study of two liver basic fatty acid-binding proteins., Di Pietro SM, Perduca M, Santome JA, Monaco HL, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1903-5. Epub 2001, Nov 21. PMID:11717512

Page seeded by OCA on Tue Jul 29 09:46:06 2008

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OCA

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 {{STRUCTURE_2ft9|  PDB=2ft9  |  SCENE=  }}
-'''Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid'''
+===Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic acid===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_16555310}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16555310 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16555310}}
 ==About this Structure==
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 ==Reference==
 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:[http://www.ncbi.nlm.nih.gov/pubmed/16555310 16555310]
+Crystallization and preliminary X-ray study of two liver basic fatty acid-binding proteins., Di Pietro SM, Perduca M, Santome JA, Monaco HL, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1903-5. Epub 2001, Nov 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11717512 11717512]
 [[Category: Ambystoma mexicanum]]
 [[Category: Single protein]]
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 [[Category: Liver basic fatty acid-binding protein]]
 [[Category: Liver bile acid-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:17:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:46:06 2008''