7VO7
Crystal structure of trypsin in complex with Lima bean trypsin inhibitor at 2.25A resolution.
Summary for 7VO7
| Entry DOI | 10.2210/pdb7vo7/pdb |
| Descriptor | Cationic trypsin, Bowman-Birk type proteinase inhibitor, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | protease, trypsin lima bean complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Bos taurus (cattle) More |
| Total number of polymer chains | 3 |
| Total formula weight | 53532.32 |
| Authors | Ahmad, M.S.,Akbar, Z.,Choudhary, M.I. (deposition date: 2021-10-12, release date: 2022-08-17, Last modification date: 2024-11-13) |
| Primary citation | Ahmad, M.S.,Akbar, Z.,Choudhary, M.I. Insight into the structural basis of the dual inhibitory mode of Lima bean (Phaseolus lunatus) serine protease inhibitor. Proteins, 91:22-31, 2023 Cited by PubMed Abstract: Bovine pancreatic trypsin was crystallized, in-complex with Lima bean trypsin inhibitor (LBTI) (Phaseolus lunatus L.), in the form of a ternary complex. LBTI is a Bowman-Birk-type bifunctional serine protease inhibitor, which has two independent inhibitory loops. Both of the loops can inhibit trypsin, however, only the hydrophobic loop is specific for inhibiting chymotrypsin. The structure of trypsin incomplex with the LBTI has been solved and refined at 2.25 Å resolution, in the space group P4 with R /R values of 18.1/23.3. The two binding sites of LBTI differ in only two amino acids. Lysine and leucine are the key residues of the two different binding loops positioned at the P1, and involved in binding the S1 binding site of trypsin. The asymmetric unit cell contains two molecules of trypsin and one molecule of LBTI. The key interactions include hydrogen bonds between LBTI and active site residues of trypsin. The 3D structure of the enzyme-inhibitor complex provided details insight into the trypsin inhibition by LBTI. To the best of our knowledge, this is the first report on the structure of trypsin incomplex with LBTI. PubMed: 35927030DOI: 10.1002/prot.26407 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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