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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 1 - Protein Evolution (A. Lupas)     Display Documents



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ID: 635927.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
Structure and function of tripeptidyl peptidase II, a giant cytosolic protease
Authors:Rockel, B.; Kopec, K. O.; Lupas, A. N.; Baumeister, W.
Date of Publication (YYYY-MM-DD):2012-01
Title of Journal:Biochim Biophys Acta
Volume:1824
Issue / Number:1
Start Page:237
End Page:245
Review Status:not specified
Audience:Not Specified
Abstract / Description:Tripeptidyl peptidase II is the largest known eukaryotic peptidase. It has been described as a multi-purpose peptidase, which, in addition to its house-keeping function in intracellular protein degradation, plays a role in several vital cellular processes such as antigen processing, apoptosis, or cell division, and is involved in diseases like muscle wasting, obesity, and in cancer. Biochemical studies and bioinformatics have identified TPPII as a subtilase, but its structure is very unusual: it forms a large homooligomeric complex (6 MDa) with a spindle-like shape. Recently, the high-resolution structure of TPPII homodimers (300 kDa) was solved and a hybrid structure of the holocomplex built of 20 dimers was obtained by docking it into the EM-density. Here, we summarize our current knowledge about TPPII with a focus on structural aspects. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome.
Free Keywords:Amino Acid Sequence; Aminopeptidases/*chemistry/genetics/metabolism/*physiology; Animals; Cytosol/enzymology/metabolism; Dipeptidyl-Peptidases and; Tripeptidyl-Peptidases/*chemistry/genetics/metabolism/*physiology; Humans; Models, Biological; Models, Molecular; Molecular Sequence Data; Peptide Hydrolases/chemistry/metabolism/physiology; Phylogeny; Protein Conformation; Proteolysis; Sequence Homology, Amino Acid; Serine Endopeptidases/*chemistry/genetics/metabolism/*physiology; Structure-Activity Relationship
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
External Affiliations:%G eng
Identifiers:ISSN:0006-3002 (Print) 0006-3002 (Linking) %R 10.1016/j... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/21771670 [ID No:2]
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