8IYV
Crystal structure of trypsin-famotidine complex at 2.10 Angstroms resolution
Summary for 8IYV
| Entry DOI | 10.2210/pdb8iyv/pdb |
| Descriptor | Cationic trypsin, SULFATE ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 23835.34 |
| Authors | Ahmad, M.S.,Kalam, N.,Akbar, Z.,Rasheed, S.,Choudhary, M.I. (deposition date: 2023-04-06, release date: 2024-09-18, Last modification date: 2024-10-30) |
| Primary citation | Ahmad, M.S.,Kalam, N.,Akbar, Z.,Shah, N.,Rasheed, S.,Choudhary, M.I. Structural basis for the binding of famotidine, cimetidine, guanidine, and pimagedine with serine protease. Biochem.Biophys.Res.Commun., 733:150603-150603, 2024 Cited by PubMed Abstract: Serine proteases are among the important groups of enzymes having significant roles in cell biology. Trypsin is a representative member of the serine superfamily of enzymes, produced by acinar cells of pancreas. It is a validated drug target for various ailments including pancreatitis and colorectal cancer. Premature activation of trypsin is involved in the lysis of pancreatic tissues, which causes pancreatitis. It is also reported to be involved in colorectal carcinoma by activating other proteases, such as matrix metalloproteinase (MMPs). The development of novel trypsin inhibitors with good pharmacokinetic properties could play important roles in pharmaceutical sciences. This study reports the crystal structures of bovine pancreatic trypsin with four molecules; cimetidine, famotidine, pimagedine, and guanidine. These compounds possess binding affinity towards the active site (S1) of trypsin. The structures of all four complexes provided insight of the binding of four different ligands, as well as the dynamics of the active site towards the bind with different size ligands. This study might be helpful in designing of new potent inhibitors of trypsin and trypsin like serine proteases. PubMed: 39216203DOI: 10.1016/j.bbrc.2024.150603 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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