Site-directed mutagenesis of rat cellular retinol-binding protein
نویسندگان
چکیده
منابع مشابه
Engineering protein mechanics: inhibition of concerted motions of the cellular retinol binding protein by site-directed mutagenesis.
Recently we reported on the dynamic properties of the cellular retinol binding protein, a member of the fatty acid binding protein family. A few conserved glycines were identified as important for producing the conformational changes necessary for the uptake and release of retinol. Here, we describe a multidisciplinary analysis of a genetically engineered mutation of one of these glycines (Gly6...
متن کاملStructure-function studies on human retinol-binding protein using site-directed mutagenesis.
Retinol-binding protein (RBP) transports vitamin A in the plasma. It consists of eight anti-parallel beta-strands (A to H) that fold to form an orthogonal barrel. The loops connecting the strands A and B, C and D, and E and F form the entrance to the binding site in the barrel. The retinol molecule is found deep inside this barrel. Apart from its specific interaction with retinol, RBP is involv...
متن کاملLocalization of cellular retinol-binding protein in several rat tissues.
The distribution of cellular retinol-binding protein (CRBP) in rat liver, ileum, and epididymis was examined by the peroxidase-antiperoxidase immunolocalization technique. Positive cytoplasmic staining was seen in the liver when antiserum prepared against purified CRBP was used but not when antiserum absorbed with purified CRBP was used. Ileal mucosa, a tissue that contains no detectable CRBP, ...
متن کاملBinding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics.
The structure and backbone dynamics of rat holo cellular retinol-binding protein II (holo-CRBP II) in solution has been determined by multidimensional NMR. The final structure ensemble was based on 3980 distance and 30 dihedral angle restraints, and was calculated using metric matrix distance geometry with pairwise Gaussian metrization followed by simulated annealing. The average RMS deviation ...
متن کاملSite-directed mutagenesis of proposed active-site residues of penicillin-binding protein 5 from Escherichia coli.
Alignment of the amino acid sequence of penicillin-binding protein 5 (PBP5) with the sequences of other members of the family of active-site-serine penicillin-interacting enzymes predicted the residues playing a role in the catalytic mechanism of PBP5. Apart from the active-site (Ser44), Lys47, Ser110-Gly-Asn, Asp175 and Lys213-Thr-Gly were identified as the residues making up the conserved box...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)64368-x