Structural highlights
Function
[BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The complex formed between anionic salmon trypsin (ST) and bovine pancreatic trypsin inhibitor (BPTI) has been crystallised, and the X-ray structure has been solved using the molecular replacement method. The crystals are hexagonal and belong to space group P6(1)22 with lattice parameters of a = b = 83.12 A and c = 222.15 A. Data have been collected to 2.1 A and the structure has been refined to a crystallographic R-factor of 20.6%. Catalysis by salmon trypsin is distinguished by a Km value 20-fold lower than that for mammalian trypsins, and a k(cat) twice as high. The present ST-BPTI complex serves as a model for the Michaelis-Menten complex, and has been compared with corresponding bovine and rat trypsin (RT) complexes. The binding of BPTI to salmon trypsin is characterised by stronger primary interactions in the active site, and a somewhat looser secondary binding.
The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor.,Helland R, Leiros I, Berglund GI, Willassen NP, Smalas AO Eur J Biochem. 1998 Sep 1;256(2):317-24. PMID:9760170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Helland R, Leiros I, Berglund GI, Willassen NP, Smalas AO. The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur J Biochem. 1998 Sep 1;256(2):317-24. PMID:9760170
