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

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About: A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases
Creator	Wlodawer, Alexander Li, Mi Oda, Kohei Oyama, Hiroshi Dunn, Ben »more»
source	Medline; PMC
abstract	BACKGROUND: Tripeptidyl-peptidase I, also known as CLN2, is a member of the family of sedolisins (serine-carboxyl peptidases). In humans, defects in expression of this enzyme lead to a fatal neurodegenerative disease, classical late-infantile neuronal ceroid lipofuscinosis. Similar enzymes have been found in the genomic sequences of several species, but neither systematic analyses of their distribution nor modeling of their structures have been previously attempted. RESULTS: We have analyzed the presence of orthologs of human CLN2 in the genomic sequences of a number of eukaryotic species. Enzymes with sequences sharing over 80% identity have been found in the genomes of macaque, mouse, rat, dog, and cow. Closely related, although clearly distinct, enzymes are present in fish (fugu and zebra), as well as in frogs (Xenopus tropicalis). A three-dimensional model of human CLN2 was built based mainly on the homology with Pseudomonas sp. 101 sedolisin. CONCLUSION: CLN2 is very highly conserved and widely distributed among higher organisms and may play an important role in their life cycles. The model presented here indicates a very open and accessible active site that is almost completely conserved among all known CLN2 enzymes. This result is somehow surprising for a tripeptidase where the presence of a more constrained binding pocket was anticipated. This structural model should be useful in the search for the physiological substrates of these enzymes and in the design of more specific inhibitors of CLN2.
has issue date	2003-11-11(xsd:dateTime)
bibo:doi	10.1186/1472-6807-3-8
bibo:pmid	14609438
has license	no-cc
sha1sum (hex)	dab2d95da5307c840eb4a1e00f0186022541d63d
schema:url	https://doi.org/10.1186/1472-6807-3-8
resource representing a document's title	A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases
has PubMed Central identifier	PMC280685
has PubMed identifier	14609438
schema:publication	BMC Struct Biol
resource representing a document's body	covid:dab2d95da5307c840eb4a1e00f0186022541d63d#body_text
is schema:about of	named entity 'PEPTIDASES' named entity 'peptidases' named entity 'defects' named entity 'structures' named entity 'peptidases' »more»

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