 |
PDBsum entry 1pi2
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Serine proteinase inhibitor
|
PDB id
|
|
|
|
1pi2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
J Biol Chem
267:1990-1994
(1992)
|
|
PubMed id:
|
|
|
|
|
| |
|
Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
|
|
P.Chen,
J.Rose,
R.Love,
C.H.Wei,
B.C.Wang.
|
|
|
|
| |
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.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
A.Clemente,
F.J.Moreno,
M.d.e.l. .C.Marín-Manzano,
E.Jiménez,
and
C.Domoney
(2010).
The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases.
|
| |
Mol Nutr Food Res,
54,
396-405.
|
 |
|
|
|
|
 |
G.F.Esteves,
R.C.Teles,
N.S.Cavalcante,
D.Neves,
M.M.Ventura,
J.A.Barbosa,
and
S.M.de Freitas
(2007).
Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
1087-1090.
|
 |
|
|
|
|
 |
J.A.Barbosa,
L.P.Silva,
R.C.Teles,
G.F.Esteves,
R.B.Azevedo,
M.M.Ventura,
and
S.M.de Freitas
(2007).
Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases.
|
| |
Biophys J,
92,
1638-1650.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
A.M.Jaulent,
A.B.Brauer,
S.J.Matthews,
and
R.J.Leatherbarrow
(2005).
Solution structure of a novel C2-symmetrical bifunctional bicyclic inhibitor based on SFTI-1.
|
| |
J Biomol NMR,
33,
57-62.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
R.F.Qi,
Z.W.Song,
and
C.W.Chi
(2005).
Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application.
|
| |
Acta Biochim Biophys Sin (Shanghai),
37,
283-292.
|
 |
|
|
|
|
 |
Y.Mao,
C.Lai,
G.Vogtentanz,
B.Schmidt,
T.Day,
J.Miller,
D.L.Brandon,
and
D.Chen
(2005).
Monoclonal antibodies against soybean Bowman-Birk inhibitor recognize the protease-reactive loops.
|
| |
Protein J,
24,
275-282.
|
 |
|
|
|
|
 |
J.A.Barbosa,
R.C.Teles,
V.P.Forrer,
B.G.Guimarães,
F.J.Medrano,
M.M.Ventura,
and
S.M.Freitas
(2003).
Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine beta-trypsin.
|
| |
Acta Crystallogr D Biol Crystallogr,
59,
1828-1830.
|
 |
|
|
|
|
 |
J.E.Debreczeni,
G.Bunkóczi,
B.Girmann,
and
G.M.Sheldrick
(2003).
In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case.
|
| |
Acta Crystallogr D Biol Crystallogr,
59,
393-395.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
W.B.Armstrong,
X.S.Wan,
A.R.Kennedy,
T.H.Taylor,
and
F.L.Meyskens
(2003).
Development of the Bowman-Birk inhibitor for oral cancer chemoprevention and analysis of Neu immunohistochemical staining intensity with Bowman-Birk inhibitor concentrate treatment.
|
| |
Laryngoscope,
113,
1687-1702.
|
 |
|
|
|
|
 |
A.Heifetz,
E.Katchalski-Katzir,
and
M.Eisenstein
(2002).
Electrostatics in protein-protein docking.
|
| |
Protein Sci,
11,
571-587.
|
 |
|
|
|
|
 |
J.D.McBride,
E.M.Watson,
A.B.Brauer,
A.M.Jaulent,
and
R.J.Leatherbarrow
(2002).
Peptide mimics of the Bowman-Birk inhibitor reactive site loop.
|
| |
Biopolymers,
66,
79-92.
|
 |
|
|
|
|
 |
E.Smyth,
C.D.Syme,
E.W.Blanch,
L.Hecht,
M.Vasák,
and
L.D.Barron
(2001).
Solution structure of native proteins with irregular folds from Raman optical activity.
|
| |
Biopolymers,
58,
138-151.
|
 |
|
|
|
|
 |
S.Krauchenco,
J.A.Silva,
R.A.Nagem,
J.R.Brandão Neto,
V.P.Forrer,
R.Carmona E Ferreira,
M.L.Macedo,
J.C.Novello,
S.Marangoni,
and
I.Polikarpov
(2001).
Crystallization and preliminary X-ray diffraction analysis of a novel trypsin inhibitor from seeds of Copaifera langsdorffii.
|
| |
Acta Crystallogr D Biol Crystallogr,
57,
1316-1318.
|
 |
|
|
|
|
 |
J.D.McBride,
H.N.Freeman,
and
R.J.Leatherbarrow
(2000).
Identification of chymotrypsin inhibitors from a second-generation template assisted combinatorial peptide library.
|
| |
J Pept Sci,
6,
446-452.
|
 |
|
|
|
|
 |
J.Leluk
(2000).
A non-statistical approach to protein mutational variability.
|
| |
Biosystems,
56,
83-93.
|
 |
|
|
|
|
 |
C.Wu,
C.Maurer,
Y.Wang,
S.Xue,
and
D.L.Davis
(1999).
Water pollution and human health in China.
|
| |
Environ Health Perspect,
107,
251-256.
|
 |
|
|
|
|
 |
H.M.Krishna Murthy,
K.Judge,
L.DeLucas,
S.Clum,
and
R.Padmanabhan
(1999).
Crystallization, characterization and measurement of MAD data on crystals of dengue virus NS3 serine protease complexed with mung-bean Bowman-Birk inhibitor.
|
| |
Acta Crystallogr D Biol Crystallogr,
55,
1370-1372.
|
 |
|
|
|
|
 |
J.K.Dattagupta,
A.Podder,
C.Chakrabarti,
U.Sen,
D.Mukhopadhyay,
S.K.Dutta,
and
M.Singh
(1999).
Refined crystal structure (2.3 A) of a double-headed winged bean alpha-chymotrypsin inhibitor and location of its second reactive site.
|
| |
Proteins,
35,
321-331.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
K.N.Rao,
S.S.Hegde,
R.J.Lewis,
and
C.G.Suresh
(1999).
Crystallization and preliminary x-ray diffraction studies of a Bowman-Birk inhibitor from Vigna unguiculata seeds.
|
| |
Acta Crystallogr D Biol Crystallogr,
55,
1920-1922.
|
 |
|
|
|
|
 |
Y.S.Kim,
H.K.Song,
and
S.W.Suh
(1999).
Crystallization and preliminary X-ray analysis of a complex between the Bowman-Birk trypsin inhibitor from barley and porcine pancreatic trypsin.
|
| |
Acta Crystallogr D Biol Crystallogr,
55,
1244-1246.
|
 |
|
|
|
|
 |
H.K.Song,
and
S.W.Suh
(1998).
Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds.
|
| |
Acta Crystallogr D Biol Crystallogr,
54,
441-443.
|
 |
|
|
|
|
 |
N.Gueven,
K.Dittmann,
C.Mayer,
and
H.P.Rodemann
(1998).
The radioprotective potential of the Bowman-Birk protease inhibitor is independent of its secondary structure.
|
| |
Cancer Lett,
125,
77-82.
|
 |
|
|
|
|
 |
B.Prakash,
S.Selvaraj,
M.R.Murthy,
Y.N.Sreerama,
D.R.Rao,
and
L.R.Gowda
(1996).
Analysis of the amino acid sequences of plant Bowman-Birk inhibitors.
|
| |
J Mol Evol,
42,
560-569.
|
 |
|
|
|
|
 |
P.G.de Carvalho,
C.Bloch,
L.Morhy,
M.C.da Silva,
L.V.de Mello,
and
G.Neshich
(1996).
Amino acid sequence of the Phaseolus vulgaris var. "fogo na serra" inhibitor and interactive surface modeling for the enzyme-inhibitor complex.
|
| |
J Protein Chem,
15,
591-598.
|
 |
|
|
|
|
 |
R.H.Voss,
U.Ermler,
L.O.Essen,
G.Wenzl,
Y.M.Kim,
and
P.Flecker
(1996).
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation.
|
| |
Eur J Biochem,
242,
122-131.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
K.Huang,
N.C.Strynadka,
V.D.Bernard,
R.J.Peanasky,
and
M.N.James
(1994).
The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase.
|
| |
Structure,
2,
679-689.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
G.Lin,
W.Bode,
R.Huber,
C.Chi,
and
R.A.Engh
(1993).
The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin.
|
| |
Eur J Biochem,
212,
549-555.
|
 |
|
PDB code:
|
 |
|
|
 |
 |
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
');
}
}
 |