1WO9
Selective inhibition of trypsins by insect peptides: role of P6-P10 loop
Summary for 1WO9
| Entry DOI | 10.2210/pdb1wo9/pdb |
| Descriptor | trypsin inhibitor (1 entity in total) |
| Functional Keywords | hydrolase inhibitor |
| Total number of polymer chains | 1 |
| Total formula weight | 3727.26 |
| Authors | Kellenberger, C.,Ferrat, G.,Leone, P.,Darbon, H.,Roussel, A. (deposition date: 2004-08-12, release date: 2004-09-07, Last modification date: 2024-10-30) |
| Primary citation | Kellenberger, C.,Ferrat, G.,Leone, P.,Darbon, H.,Roussel, A. Selective inhibition of trypsins by insect peptides: role of P6-P10 loop Biochemistry, 42:13605-13612, 2003 Cited by PubMed Abstract: PMP-D2 and HI, two peptides from Locusta migratoria, were shown to belong to the family of tight-binding protease inhibitors. However, they interact weakly with bovine trypsin (K(i) around 100 nM) despite a trypsin-specific Arg at the primary specificity site P1. Here we demonstrate that they are potent inhibitors of midgut trypsins isolated from the same insect and of a fungal trypsin from Fusarium oxysporum (K(i) DOI: 10.1021/bi035318t PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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