Linked Life Data

1761542

Source:http://linkedlifedata.com/resource/pubmed/id/1761542

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1992-2-7
pubmed:abstractText
Rat cellular retinol-binding protein II (CRBP II) is an abundant 134-residue intestinal protein that binds all-trans-retinol and all-trans-retinal. It belongs to a family of homologous, 15-kDa cytoplasmic proteins that bind hydrophobic ligands in a noncovalent fashion. These binding proteins include a number of proteins that bind long chain fatty acids. X-ray analyses of the structure of two family members, rat intestinal fatty acid-binding protein and bovine myelin P2 protein, indicate that they have a high degree of conformational similarity and that the carboxylate group of their bound fatty acid interacts with a delta-guanidium group of at least 1 of 2 "buried" arginine residues. These 2 Arg residues are conserved in other family members that bind long chain fatty acids and in cellular retinoic acid-binding protein, but are replaced by Gln109 and Gln129 in CRBP II. We have genetically engineered two amino acid substitutions in CRBP II: 1) Gln109 to Arg and 2) Gln129 to Arg. The purified Escherichia coli-derived CRBP II mutant proteins were analyzed by fluorescence and nuclear magnetic resonance spectroscopy. Both mutants exhibit markedly decreased binding of all-trans-retinol and all-trans-retinaldehyde, but no increased binding of all-trans-retinoic acid. Arg substitution for Gln109 but not for Gln129 produces a dramatic increase in palmitate binding activity. Analysis of the endogenous fatty acids associated with the purified E. coli-derived proteins revealed that E. coli-derived intestinal fatty acid binding protein and the Arg109 CRBP II mutant are complexed with endogenous fatty acids in a qualitatively and quantitatively similar manner. These results provide evidence that this internal Arg may play an important role in the binding of long chain fatty acids by members of this protein family.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24404-12
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:1761542-Amino Acid Sequence, pubmed-meshheading:1761542-Animals, pubmed-meshheading:1761542-Base Sequence, pubmed-meshheading:1761542-Carrier Proteins, pubmed-meshheading:1761542-Cattle, pubmed-meshheading:1761542-Fatty Acid-Binding Proteins, pubmed-meshheading:1761542-Fatty Acids, pubmed-meshheading:1761542-Fluorine, pubmed-meshheading:1761542-Magnetic Resonance Spectroscopy, pubmed-meshheading:1761542-Molecular Sequence Data, pubmed-meshheading:1761542-Mutagenesis, Site-Directed, pubmed-meshheading:1761542-Myelin Proteins, pubmed-meshheading:1761542-Neoplasm Proteins, pubmed-meshheading:1761542-Nerve Tissue Proteins, pubmed-meshheading:1761542-Protein Conformation, pubmed-meshheading:1761542-Rats, pubmed-meshheading:1761542-Retinol-Binding Proteins, pubmed-meshheading:1761542-Retinol-Binding Proteins, Cellular, pubmed-meshheading:1761542-Sequence Alignment, pubmed-meshheading:1761542-Substrate Specificity
pubmed:year
1991
pubmed:articleTitle
Alteration of the binding specificity of cellular retinol-binding protein II by site-directed mutagenesis.
pubmed:affiliation
Department of Medicine, Washington University, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't