Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases (Articolo in rivista) (literal)

Anno

• 2001-01-01T00:00:00+01:00 (literal)

Alternative label

• Turk, D., Janjic, V., Stern, I., Podobnik, M., Lamba, D., Dahl, S.W., Lauritzen, C., Pedersen, J., Turk, V., Turk, B. (2001)
  Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
  in EMBO journal (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Turk, D., Janjic, V., Stern, I., Podobnik, M., Lamba, D., Dahl, S.W., Lauritzen, C., Pedersen, J., Turk, V., Turk, B. (literal)

Pagina inizio

• 6570 (literal)

Pagina fine

• 6582 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 20 (literal)

Rivista

• EMBO journal (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 13 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 23 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Turk, D. - Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia Janjic, V. - Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia Stern, I. - Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia Podobnik, M. - Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia Lamba, D. - CNR - Istituto di Cristallografia, UOS Trieste, Italia Dahl, S.W. - Unizyme Laboratories A/S, Hoersholm, Denmark Lauritzen, C. - Unizyme Laboratories A/S, Hoersholm, Denmark Pedersen, J. - Unizyme Laboratories A/S, Hoersholm, Denmark Turk, V. - Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia Turk, B. - Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia (literal)

Titolo

• Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases (literal)

Abstract

• Dipeptidyl peptidase I (DPPI) or cathepsin C is the physiological activator of groups of serine proteases from immune and inflammatory cells vital for defense of an organism. The structure presented shows how an additional domain transforms the framework of a papain-like endopeptidase into a robust oligomeric protease-processing enzyme. The tetrahedral arrangement of the active sites exposed to solvent allows approach of proteins in their native state; the massive body of the exclusion domain fastened within the tetrahedral framework excludes approach of a polypeptide chain apart from its termini;, and the carboxylic group of Asp1 positions the N-terminal amino group of the substrate. Based on a structural comparison and interactions within the active site cleft, it is suggested that the exclusion domain originates from a metallo-protease inhibitor. The location of missense mutations, characterized in people suffering from Haim-Munk and Papillon-Lefevre syndromes, suggests how they disrupt the fold and function of the enzyme. (literal)

Prodotto di

• Studi strutturali e funzionali di proteine di interesse biomedico e biotecnologico (PM.P01.023.001) (Modulo)
• Institute of Crystallography (IC) (Istituto)

Autore CNR

• DORIANO LAMBA (Unità di personale interno)

Insieme di parole chiave

• Parole chiave di "Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of Crystallography (IC) (Istituto)
• Studi strutturali e funzionali di proteine di interesse biomedico e biotecnologico (PM.P01.023.001) (Modulo)

Autore CNR di

• DORIANO LAMBA (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• EMBO journal (Rivista)

Insieme di parole chiave di

• Parole chiave di "Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases" (Insieme di parole chiave)