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 structure of bovine pancreatic trypsin inhibitor (BPTI) has been solved at 2.1 A resolution in a new crystal form (space group P6422 with unit-cell dimensions a = b = 95.0, c = 158.1 A). The asymmetric unit is a pentamer, but a decamer is created by application of crystallographic symmetry. The decamer of BPTI is only the fourth such assembly reported to date in the Protein Data Bank.
Decamers observed in the crystals of bovine pancreatic trypsin inhibitor.,Lubkowski J, Wlodawer A Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):335-7. Epub 1999, Jan 1. PMID:10089443[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lubkowski J, Wlodawer A. Decamers observed in the crystals of bovine pancreatic trypsin inhibitor. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):335-7. Epub 1999, Jan 1. PMID:10089443 doi:10.1107/S0907444998011068
