7Z9F
Human anionic trypsin after autoproteolysis at Arg122
Summary for 7Z9F
| Entry DOI | 10.2210/pdb7z9f/pdb |
| Descriptor | Trypsin-2, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | try2, serine protease, autoproteolysis, digestion, hydrolase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 48237.86 |
| Authors | Nagel, F.,Palm, G.J.,Delcea, M.,Lammers, M. (deposition date: 2022-03-21, release date: 2022-06-29, Last modification date: 2024-10-09) |
| Primary citation | Nagel, F.,Susemihl, A.,Geist, N.,Mohlis, K.,Palm, G.J.,Lammers, M.,Delcea, M. Structural Basis of the Pancreatitis-Associated Autoproteolytic Failsafe Mechanism in Human Anionic Trypsin. J Inflamm Res, 15:3633-3642, 2022 Cited by PubMed Abstract: The pathophysiological mechanisms underlying chronic pancreatitis (CP) are still poorly understood. Human cationic (TRY1) and anionic (TRY2) trypsins are the two major trypsin isoforms and their activities are tightly regulated within pancreatic acinar cells. Typically, they exist in a molar ratio of 2:1 (cationic:anionic). This ratio is reversed during chronic alcohol abuse, pancreatic cancer, or pancreatitis due to selectively upregulated expression of TRY2, causing anionic trypsin to become the predominant isoform. The involvement of TRY2 in pancreatitis is considered limited due to the absence of disease-causing mutations and its increased prevalence for autoproteolysis. However, exacerbated pancreatitis in TRY2 overexpressing mice was recently demonstrated. Here, we aim to elucidate the molecular structure of human anionic trypsin and obtain insights into the autoproteolytic regulation of tryptic activity. PubMed: 35775010DOI: 10.2147/JIR.S367699 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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