Scrambled isomers as key intermediates in the oxidative folding of ligand binding module 5 of the low density lipoprotein receptor

Journal of Biological Chemistry

Volumn 283, Issue 20, 2008, Pages 13627-13637

  Arias Moreno, Xabier ^a   Arolas, Joan L ^b   Aviles, Francesc X ^b   Sancho, Javier ^a   Ventura, Salvador ^b  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; CALCIUM; CALCIUM ALLOYS; CATALYST ACTIVITY; COORDINATION REACTIONS; ISOMERS; LIGANDS; RATE CONSTANTS; STRUCTURAL ANALYSIS;

CALCIUM BINDING MOTIFS; COMPETENT CONFORMATIONS; DISULFIDE BONDS; DO-MAINS; ENERGY MINIMUMS; FOLDING PATHWAYS; FOLDING PROCESSES; FOLDING REACTIONS; FUNCTIONAL CONFORMATIONS; HYPERCHOLESTEROLEMIA; ION FUNNELS; KEY INTERMEDIATES; LIGAND BINDINGS; LIMITING STEPS; LOW DENSITY LIPOPROTEIN RECEPTORS; MOLECULAR BASES; NATIVE FORMS; NATIVE STATES; OXIDATIVE FOLDING; REACTIVE CYSTEINES; SEQUENTIAL OXIDATIONS; UNFOLDING PATHWAYS; WILD TYPES;

PROTEIN FOLDING;

BINDING PROTEIN; CALCIUM; CYSTEINE; LIGAND BINDING MODULE 5 PROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; MUTANT PROTEIN; UNCLASSIFIED DRUG; ISOPROTEIN; OXYGEN;

ARTICLE; DISULFIDE BOND; FAMILIAL HYPERCHOLESTEROLEMIA; ISOMER; LIGAND BINDING; OXIDATION; OXIDATIVE FOLDING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STABILITY; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; GENE EXPRESSION REGULATION; HUMAN; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CYSTEINE; GENE EXPRESSION REGULATION; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; OXYGEN; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, LDL;

EID: 46649108197     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M800755200     Document Type: Article

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