1tw4: Difference between revisions

Revision as of 04:53, 28 July 2008

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File:1tw4.png

Template:STRUCTURE 1tw4

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

Template:ABSTRACT PUBMED 15518556

About this StructureAbout this Structure

1TW4 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

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:15518556

Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 A resolution., Scapin G, Spadon P, Mammi M, Zanotti G, Monaco HL, Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):95-9. PMID:2266974

Chicken liver basic fatty acid-binding protein (pI = 9.0). Purification, crystallization and preliminary X-ray data., Scapin G, Spadon P, Pengo L, Mammi M, Zanotti G, Monaco HL, FEBS Lett. 1988 Nov 21;240(1-2):196-200. PMID:3191992

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OCA

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-'''Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid'''
+===Crystal Structure of Chicken Liver Basic Fatty Acid Binding Protein (Bile Acid Binding Protein) Complexed With Cholic Acid===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15518556}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15518556 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15518556}}
 ==About this Structure==
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 ==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]
+Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 A resolution., Scapin G, Spadon P, Mammi M, Zanotti G, Monaco HL, Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):95-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2266974 2266974]
+Chicken liver basic fatty acid-binding protein (pI = 9.0). Purification, crystallization and preliminary X-ray data., Scapin G, Spadon P, Pengo L, Mammi M, Zanotti G, Monaco HL, FEBS Lett. 1988 Nov 21;240(1-2):196-200. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3191992 3191992]
 [[Category: Gallus gallus]]
 [[Category: Single protein]]
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 [[Category: Intracellular bile acid-binding protein]]
 [[Category: Lb-fabp]]
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