Structure of the LDL receptor extracellular domain at endosomal pH

Science

Volumn 298, Issue 5602, 2002, Pages 2353-2358

  Rudenko, Gabby ^a   Henry, Lisa ^a,b   Henderson, Keith ^b   Ichtchenko, Konstantin ^a,c   Brown, Michael S ^a   Goldstein, Joseph L ^a   Deisenhofer, Johann ^a,b  

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

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CHOLESTEROL; CRYSTAL GROWTH; CRYSTAL STRUCTURE; EPIDEMIOLOGY; PH;

LOW-DENSITY LIPOPROTEINS (LDL);

PROTEINS;

CALCIUM BINDING PROTEIN; CHOLESTEROL; EPIDERMAL GROWTH FACTOR; LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR;

CRYSTAL STRUCTURE; PROTEIN;

ARTICLE; CELL PH; CRYSTAL STRUCTURE; ENDOSOME; EXTRACELLULAR SPACE; HOMEOSTASIS; HUMAN; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECRETION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ENDOSOMES; EPIDERMAL GROWTH FACTOR; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; LIGANDS; LIPOPROTEINS, LDL; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, LDL; REPETITIVE SEQUENCES, AMINO ACID;

EID: 0037147281     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1078124     Document Type: Article

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53. We thank the staff at the synchrotrons APS ID-19 and ALS 5.0.2 and 8.2.1 for excellent support, Y. Chelliah for initial studies on the insect cell overexpression system, M. Machius and R. Sunahara for crucial discussions, and T. C. Südhof and M. Machius for reviewing the manuscript. J.L.G. and M.S.B. acknowledge the support of grants from the NIH (HL20948) and the Perot Family Foundation. The atomic coordinates have been deposited to the Protein Data Bank, accession code 1N7D.