Tpp1 Protein (Tripeptidyl Peptidase 1) is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
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| Attribute | Value |
|---|---|
| Protein Name | Tripeptidyl Peptidase 1 |
| Gene | TPP1 |
| UniProt ID | O14773 |
| PDB Structure | 3EDY, 4ATG |
| Molecular Weight | 59 kDa |
| Subcellular Localization | Lysosomal lumen |
| Protein Family | S9 family serine proteases |
TPP1 (Tripeptidyl Peptidase 1) is a lysosomal serine protease that cleaves tripeptides from the N-terminus of proteins. It is the major exopeptidase in lysosomes and plays a critical role in protein degradation. Mutations in TPP1 cause Late Infantile Neuronal Ceroid Lipofuscinosis (LINCL)[1].
TPP1 is a 563-amino acid glycoprotein:
TPP1 structure (PDB: 3EDY):
TPP1 is a serine protease with unique tripeptidyl-peptidase activity:
TPP1 degrades:
TPP1 mutations cause LINCL (also known as CLN2 disease)[1]:
TPP1 deficiency causes:
Cerliponase alfa (Brineura) - First disease-modifying therapy for LINCL:
The study of Tpp1 Protein (Tripeptidyl Peptidase 1) has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Markham A. "Cerliponase alfa: first global approval." Drugs. Drugs. 2017. ↩︎