Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis

Journal of Biological Chemistry

Volumn 284, Issue 6, 2009, Pages 3976-3984

  Pal, Aritra ^a   Kraetzner, Ralph ^a   Gruene, Tim ^a   Grapp, Marcel ^a   Schreiber, Kathrin ^a   Grønborg, Mads ^b   Urlaub, Henning ^b   Becker, Stefan ^b   Asif, Abdul R ^a   Gärtner, Jutta ^a   Sheldrick, George M ^a   Steinfeld, Robert ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOCATALYTIC; AUTOPROCESSING; CATALYTIC DOMAINS; CATALYTIC TRIAD; CEROID LIPOFUSCINOSIS; GLOBULAR STRUCTURE; GLYCOSYLATED; IN-VITRO; MOLECULAR BASIS; NEURODEGENERATIVE DISEASE; OCTAHEDRALLY COORDINATED; STERIC CONSTRAINT; SUBTILISIN; TRI-PEPTIDES; TRIPEPTIDYL-PEPTIDASE I; X-RAY CRYSTALLOGRAPHIC ANALYSIS;

BINDING ENERGY; CALCIUM; GENE ENCODING;

BINDING SITES;

ASPARTIC ACID; CALCIUM ION; GLUTAMIC ACID; PEPTIDASE; PROTEIN S53; SERINE; SERINE PROTEINASE; SUBTILISIN; TRIPEPTIDYL PEPTIDASE I; UNCLASSIFIED DRUG; PROTEINASE; TRIPEPTIDYL-PEPTIDASE I;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME GLYCOSYLATION; ENZYME STRUCTURE; HUMAN; HUMAN CELL; MISSENSE MUTATION; NEURONAL CEROID LIPOFUSCINOSIS; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY; CELL LINE; CHEMISTRY; ENZYMOLOGY; GENETICS; GLYCOSYLATION; MUTATION; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION;

CELL LINE; CRYSTALLOGRAPHY, X-RAY; ENDOPEPTIDASES; GLYCOSYLATION; HUMANS; MUTATION; NEURONAL CEROID-LIPOFUSCINOSES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 63649148741     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M806947200     Document Type: Article

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