 |
PDBsum entry 1pi2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Serine proteinase inhibitor
|
PDB id
|
|
|
|
1pi2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Reactive sites of an anticarcinogenic bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
|
|
|
Authors
|
|
P.Chen,
J.Rose,
R.Love,
C.H.Wei,
B.C.Wang.
|
|
|
Ref.
|
|
J Biol Chem, 1992,
267,
1990-1994.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The three-dimensional structure of the Bowman-Birk type proteinase inhibitor
(PI-II) has been determined by x-ray crystallography and refined at 2.5-A
resolution. This protein is a specific inhibitor of trypsin. Two reactive site
loops, one at each end of the PI-II molecule, are structurally similar to each
other and to reactive-site loops of pancreatic secretory trypsin inhibitor
(Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos,
E., and Huber, R. (1982) J. Mol. Biol. 162, 839-869) and bovine pancreatic
trypsin inhibitor (Deisenhofer, J., and Steigemann, W. (1975) Acta Crystallogr.
B31, 238-250). PI-II is the first reported Bowman-Birk type inhibitor structure
to be refined at high resolution, providing further insight into inhibitor
mechanisms.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystallization of two cubic forms of soybean trypsin inhibitor e-I, A member of the bowman-Birk inhibitor family.
|
|
|
Author
|
|
C.H.Wei.
|
|
|
Ref.
|
|
J Biol Chem, 1983,
258,
9357-9359.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
