A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases

BMC Structural Biology

Volumn 3, Issue , 2003, Pages 1-10

  Wlodawer, Alexander ^a   Durell, Stewart R ^b   Li, Mi ^a,c   Oyama, Hiroshi ^d   Oda, Kohei ^d   Dunn, Ben M ^e  

^a NATIONAL CANCER INSTITUTE   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c SAIC FREDERICK INC   (United States)

^d KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

^e UNIVERSITY OF FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SEDOLISIN; SERINE PROTEINASE; TRIPEPTIDYL PEPTIDASE I; UNCLASSIFIED DRUG; AMINOPEPTIDASE; CARBOXYPEPTIDASE; DIPEPTIDYL PEPTIDASE; LIGAND; PEPTIDE HYDROLASE; PROTEINASE; TRIPEPTIDYL-PEPTIDASE 1;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; MOLECULAR MODEL; ORTHOLOGY; PROTEIN FAMILY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SPECIES COMPARISON; ANIMAL; BINDING SITE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DOG; ENZYMOLOGY; GENETICS; HUMAN; MACACA; MOLECULAR GENETICS; MOUSE; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN TERTIARY STRUCTURE; PSEUDOMONAS; RAT; XENOPUS; ZEBRA FISH;

ANURA; CANIS FAMILIARIS; EUKARYOTA; PSEUDOMONAS; PSEUDOMONAS SP.; PSEUDOMONAS SP. 101; TAKIFUGU; XENOPUS TROPICALIS;

AMINO ACID SEQUENCE; AMINOPEPTIDASES; ANIMALS; BINDING SITES; CARBOXYPEPTIDASES; CATTLE; CONSERVED SEQUENCE; DIPEPTIDYL-PEPTIDASES AND TRIPEPTIDYL-PEPTIDASES; DOGS; ENDOPEPTIDASES; HUMANS; LIGANDS; MACACA; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE HYDROLASES; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE PROTEASES; XENOPUS; ZEBRAFISH;

EID: 3042675464     PISSN: 14726807     EISSN: None     Source Type: Journal    
DOI: 10.1186/1472-6807-3-1     Document Type: Article

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