Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 17, 2007, Pages 7015-7020

  Bosch, Jürgen ^a,b   Buscaglia, Carlos A ^c,d   Krumm, Brian ^a   Ingason, Bjarni P ^a   Lucas, Robert ^a   Roach, Claudia ^a   Cardozo, Timothy ^c   Nussenzweig, Victor ^c   Hol, Wim G J ^a,b  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

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

^d INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS   (Argentina)

Author keywords

Actin; Apicomplexa; Cell invasion machinery; Gliding motility; Induced fit

Indexed keywords

ARGININE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUTAMIC ACID; GLUTAMINE; HELIX LOOP HELIX PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; PROTEIN; THROMBOSPONDIN RELATED ANONYMOUS PROTEIN; UNCLASSIFIED DRUG; INDOLE; INDOLE DERIVATIVE; PROTOZOAL PROTEIN; THROMBOSPONDIN RELATED ADHESIVE PROTEIN, PROTOZOAN; THROMBOSPONDIN-RELATED ADHESIVE PROTEIN, PROTOZOAN;

ACTIN FILAMENT; APICOMPLEXA; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ERYTHROCYTE; HOST PARASITE INTERACTION; HYDROPHILICITY; HYDROPHOBICITY; NONHUMAN; PLASMODIUM; PLASMODIUM FALCIPARUM; PLASMODIUM VIVAX; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; SPOROZOITE; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; MALARIA FALCIPARUM; METABOLISM; MOLECULAR GENETICS; MUTATION; PARASITOLOGY; PATHOGENICITY; PROTEIN SECONDARY STRUCTURE;

APICOMPLEXA; PLASMODIUM (APICOMPLEXA); PLASMODIUM BERGHEI; PLASMODIUM FALCIPARUM; PLASMODIUM VIVAX;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; FRUCTOSE-BISPHOSPHATE ALDOLASE; INDOLES; MALARIA, FALCIPARUM; MOLECULAR SEQUENCE DATA; MUTATION; PLASMODIUM FALCIPARUM; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTOZOAN PROTEINS; SUBSTRATE SPECIFICITY;

EID: 34249859484     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0605301104     Document Type: Article

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