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
Crystal structures of four mutants of bovine pancreatic trypsin inhibitor (F22A, Y23A, N43G, and F45A), engineered to alter their stability properties, have been determined. The mutated residues, which are highly conserved among Kunitz-type inhibitors, are located in the rigid core of the molecule. Replacement of the partially buried bulky residues of the wild-type protein with smaller residues resulted in crevices open to the exterior of the molecule. The overall three-dimensional structure of these mutants is very similar to that of the wild-type protein and only small rearrangements are observed among the atoms lining the crevices.
Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A.,Danishefsky AT, Housset D, Kim KS, Tao F, Fuchs J, Woodward C, Wlodawer A Protein Sci. 1993 Apr;2(4):577-87. PMID:8518731[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Danishefsky AT, Housset D, Kim KS, Tao F, Fuchs J, Woodward C, Wlodawer A. Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A. Protein Sci. 1993 Apr;2(4):577-87. PMID:8518731
