2M3N
Peptide leucine arginine
Summary for 2M3N
| Entry DOI | 10.2210/pdb2m3n/pdb |
| Related | 1GM2 1JBL |
| NMR Information | BMRB: 18970 |
| Descriptor | Peptide leucine arginine (1 entity in total) |
| Functional Keywords | bowman birk inhibitor, hydrolase inhibitor |
| Biological source | Rana pipiens (Northern leopard frog) |
| Cellular location | Secreted: Q90WP7 |
| Total number of polymer chains | 1 |
| Total formula weight | 2141.60 |
| Authors | Polte, T. (deposition date: 2013-01-23, release date: 2013-09-11, Last modification date: 2024-10-30) |
| Primary citation | Rothemund, S.,Sonnichsen, F.D.,Polte, T. Therapeutic potential of the Peptide leucine arginine as a new nonplant bowman-birk-like serine protease inhibitor. J.Med.Chem., 56:6732-6744, 2013 Cited by PubMed Abstract: The peptide leucine arginine (pLR) belongs to a new class of cyclic peptides isolated from frog skin. Its primary sequence is similar to the reactive loop of plant Bowman-Birk inhibitors (BBI), and the recently discovered circular sunflower trypsin inhibitor-1 (SFTI-1). The conformational properties of pLR in solution were determined by NMR spectroscopy and revealed excellent structural similarity to BBI and SFTI-1. Moreover, pLR is a highly potent trypsin inhibitor, with Ki values in the nanomolar range, and, due to its small size, a potential inhibitor of the serine protease tryptase. Since tryptase plays a crucial role in the development of allergic airway inflammation, the therapeutic potential of pLR in a murine asthma model was investigated. Treatment of ovalbumin-sensitized mice with pLR during allergen challenge reduced the acute asthma phenotype. Most importantly, application even at the end of a long-lasting chronic asthma model decreased the development of chronic airway inflammation and tissue remodeling. PubMed: 23988198DOI: 10.1021/jm4005362 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
