دورية أكاديمية
Structure and function of tripeptidyl peptidase II, a giant cytosolic protease.
| العنوان: | Structure and function of tripeptidyl peptidase II, a giant cytosolic protease. |
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| المؤلفون: | Rockel B; Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany. rockel@biochem.mpg.de, Kopec KO, Lupas AN, Baumeister W |
| المصدر: | Biochimica et biophysica acta [Biochim Biophys Acta] 2012 Jan; Vol. 1824 (1), pp. 237-45. Date of Electronic Publication: 2011 Jul 13. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier Pub. Co. |
| مواضيع طبية MeSH: | Aminopeptidases/*chemistry , Aminopeptidases/*physiology , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/*chemistry , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/*physiology , Serine Endopeptidases/*chemistry , Serine Endopeptidases/*physiology, Amino Acid Sequence ; Aminopeptidases/genetics ; Aminopeptidases/metabolism ; Animals ; Cytosol/enzymology ; Cytosol/metabolism ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/genetics ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/metabolism ; Humans ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Peptide Hydrolases/chemistry ; Peptide Hydrolases/metabolism ; Peptide Hydrolases/physiology ; Phylogeny ; Protein Conformation ; Proteolysis ; Sequence Homology, Amino Acid ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism ; Structure-Activity Relationship |
| مستخلص: | 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. (Copyright © 2011 Elsevier B.V. All rights reserved.) |
| المشرفين على المادة: | EC 3.4.- (Peptide Hydrolases) EC 3.4.11.- (Aminopeptidases) EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases) EC 3.4.14.10 (tripeptidyl-peptidase 2) EC 3.4.21.- (Serine Endopeptidases) |
| تواريخ الأحداث: | Date Created: 20110721 Date Completed: 20120424 Latest Revision: 20161126 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/j.bbapap.2011.07.002 |
| PMID: | 21771670 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0006-3002 |
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| DOI: | 10.1016/j.bbapap.2011.07.002 |