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Titolo:
Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP) - A conserved acidic residue in the complement-type repeats is importantfor recognition of RAP
Autore:
Andersen, OM; Christensen, LL; Christensen, PA; Sorensen, ES; Jacobsen, C; Moestrup, SK; Etzerodt, M; Thogersen, HC;
Indirizzi:
Aarhus Univ, Gene Express Lab, DK-8000 Aarhus C, Denmark Aarhus Univ Aarhus Denmark C Gene Express Lab, DK-8000 Aarhus C, Denmark Aarhus Univ, Dept Biol Mol & Struct, Prot Chem Lab, DK-8000 Aarhus, Denmark Aarhus Univ Aarhus Denmark DK-8000 rot Chem Lab, DK-8000 Aarhus, Denmark Aarhus Univ, Dept Biochem Med, DK-8000 Aarhus C, Denmark Aarhus Univ Aarhus Denmark C Dept Biochem Med, DK-8000 Aarhus C, Denmark
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 28, volume: 275, anno: 2000,
pagine: 21017 - 21024
SICI:
0021-9258(20000714)275:28<21017:IOTMFU>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYSTEINE-RICH REPEAT; APOLIPOPROTEIN-E RECEPTOR-2; GROWTH-FACTOR PRECURSOR; LDL-RECEPTOR; LIGAND-BINDING; ALPHA-2-MACROGLOBULIN RECEPTOR; TERMINAL DOMAIN; HIGH-AFFINITY; 3-DIMENSIONAL STRUCTURE; MOLECULAR CHAPERONE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Thogersen, HC Aarhus Univ, Gene Express Lab, Gustav Wieds Vej 10, DK-8000 Aarhus C, Denmark Aarhus Univ Gustav Wieds Vej 10 Aarhus Denmark C C, Denmark
Citazione:
O.M. Andersen et al., "Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP) - A conserved acidic residue in the complement-type repeats is importantfor recognition of RAP", J BIOL CHEM, 275(28), 2000, pp. 21017-21024

Abstract

The low density lipoprotein receptor-related protein (LRP), a member of the low density lipoprotein receptor family, mediates the internalization of a diverse set of ligands, The ligand binding sites are located in differentregions of clusters consisting of similar to 40 residues, cysteine-rich complement-type repeats (CRs), The 39-40-kDa receptor-associated protein, a folding chaperone/escort protein required for efficient transport of functional LRP to the cell surface, is an antagonist of all identified ligands. Toanalyze the multisite inhibition by RAP in ligand binding of LRP, we have used an Escherichia coli expression system to produce fragments of the entire second ligand binding cluster of LRP (CR3-10). By ligand affinity chromatography and surface plasmon resonance analysis, we show that RAP binds to all two-repeat modules except CR910, CR10 differs from other repeats in cluster II by not containing a surface-exposed conserved acidic residue between Cys(IV) and Cys(V). By site-directed mutagenesis and ligand competition analysis, we provide evidence for a crucial importance of this conserved residue for RAP binding. We provide experimental evidence showing that two adjacent complement-type repeats, both containing a conserved acidic residue, represent a minimal unit required for efficient binding to RAP.

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Documento generato il 01/12/20 alle ore 07:45:51