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http://purl.uniprot.org/citations/3182800http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3182800http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3182800http://www.w3.org/2000/01/rdf-schema#comment"The amino acid sequences at the "proteolytic processing regions" of cathepsin Ds have been determined for the enzymes from cows, pigs, and rats in order to deduce the sites of cleavage as well as the function of the proteolytic processing of cathepsin D. For bovine cathepsin D, the "processing region" sequence was determined from a peptide isolated from the single-chain enzyme. The COOH-terminal sequence of the light chain and the NH2-terminal sequence of the heavy chain were also determined. The processing region sequence of porcine cathepsin D was determined from its cDNA structure, and the same structure from rat cathepsin D was determined from the peptide sequence of the single-chain rat enzyme. From sequence homology to other aspartic proteases whose x-ray crystallographic structures are known, such as pepsinogen and penicillopepsin, it is clear that the processing regions are insertions to form an extended beta-hairpin loop between residues 91 and 92 (porcine pepsin numbers). However, the sizes of the processing regions of cathepsin Ds from different species are considerably different. For the enzymes from rats, cows, pigs, and human, the sizes of the processing regions are 6, 9, 9, and 11 amino acid residues, respectively. The amino acid sequences within the processing regions are considerably different. In addition, the proteolytic processing sites were found to be completely different in the bovine and porcine cathepsin Ds. While in the porcine enzyme, an Asn-Ser bond and a Gly-Val bond are cleaved to release 5 residues as a consequence of the processing; in the bovine enzyme, two Ser-Ser bonds are cleaved to release 2 serine residues. These findings would argue that the in vivo proteolytic processing of the cathepsin D single chain is probably not carried out by a specific "processing protease." Model building of the cathepsin D processing region conformation was conducted utilizing the homology between procathepsin D and porcine pepsinogen. The beta-hairpin structure of the processing region was found to (i) interact with the activation peptide of the procathepsin D in a beta-structure and (ii) place the Cys residue in the processing region within disulfide linkage distance to Cys-27 of cathepsin D light chain. These observations support the view that the processing region of cathepsin D may function to stabilize the conformation of procathepsin D and may play a role in its activation."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)37621-x"xsd:string
http://purl.uniprot.org/citations/3182800http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)37621-x"xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Takahashi T."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Takahashi T."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Yonezawa S."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Yonezawa S."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Wong R.N.S."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Wong R.N.S."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Hartsuck J.A."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/author"Hartsuck J.A."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/pages"16504-16511"xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/pages"16504-16511"xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/title"Structures at the proteolytic processing region of cathepsin D."xsd:string
http://purl.uniprot.org/citations/3182800http://purl.uniprot.org/core/title"Structures at the proteolytic processing region of cathepsin D."xsd:string
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