The epidermal growth factor homology domain of the LDL receptor drives lipoprotein release through an allosteric mechanism involving H190, H562, and H586

Journal of Biological Chemistry

Volumn 283, Issue 39, 2008, Pages 26528-26537

  Zhao, Zhenze ^a   Michaely, Peter ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; CONFORMATIONS;

ALLOSTERIC MECHANISMS; CHARGED RESIDUES; COMPETITIVE MECHANISMS; CONFORMATIONAL CHANGES; CONFORMATIONAL TRANSITIONS; CURRENT MODELS; ENDOSOMES; EPIDERMAL GROWTH FACTORS; HOMOLOGY DOMAINS; IONIC CONTACTS; LDL RECEPTORS; LIPOPROTEIN BINDINGS; LOW DENSITIES; MUTAGENESIS EXPERIMENTS; RELEASE PROCESSES;

DRIVES;

ALANINE; EPIDERMAL GROWTH FACTOR; HISTIDINE; LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; VERY LOW DENSITY LIPOPROTEIN; INTERMEDIATE DENSITY LIPOPROTEIN;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HUMAN; HUMAN CELL; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN SECRETION; PROTEIN TRANSPORT; PROTON TRANSPORT; WILD TYPE; AMINO ACID SUBSTITUTION; ANIMAL; DRUG POTENTIATION; ENDOCYTOSIS; ENDOSOME; GENETICS; METABOLISM; MISSENSE MUTATION; PH; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; RABBIT; SEQUENCE HOMOLOGY;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; ANIMALS; ENDOCYTOSIS; ENDOSOMES; EPIDERMAL GROWTH FACTOR; HISTIDINE; HUMANS; HYDROGEN-ION CONCENTRATION; LIPOPROTEINS, IDL; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RABBITS; RECEPTORS, LDL; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 55549146819     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M804624200     Document Type: Article

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