Crystal Structure of Chicken Liver Basic Fatty Acid-Binding Protein complexed with cholic acid
| Autor: | Massimiliano Perduca, Maria E. Carrizo, Stefano Capaldi, Pier Giorgio Righetti, Hugo L. Monaco, Daniele Nichesola |
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| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular L-BABP Lb-FABP chicken liver basic fatty acid-binding protein Stereochemistry Protein Conformation Molecular Sequence Data Crystal structure Biology Crystallography X-Ray Fatty Acid-Binding Proteins Ligands Biochemistry Fatty acid-binding protein Bile Acids and Salts chemistry.chemical_compound Molecule Animals Amino Acid Sequence Peptide sequence Conserved Sequence chemistry.chemical_classification Binding Sites Membrane Glycoproteins Chicken Liver Basic Fatty Acid-Binding Protein Crystal Structure cholic acid Binding protein Cholic acid Space group Amino acid chemistry Liver lipids (amino acids peptides and proteins) Apoproteins Carrier Proteins Crystallization Chickens Protein Binding |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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