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PDBsum entry 2bbi
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Serine protease inhibitor
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PDB id
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2bbi
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
31:999
(1992)
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PubMed id:
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Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution.
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M.H.Werner,
D.E.Wemmer.
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ABSTRACT
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The three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk
inhibitor in solution has been determined by two-dimensional 1H nuclear magnetic
resonance spectroscopy and dynamical simulated annealing using the program
XPLOR. The structure was defined by 907 NOEs involving intra- and interresidue
contacts which served as distance constraints for a protocol of dynamical
simulated annealing. In addition, 48 phi angle constraints involving non-proline
amino acids, 29 chi angle constraints, six omega angle constraints for the X-Pro
peptide bond, and 35 stereoassignments for prochiral centers were incorporated
during the course of the calculation. The protein is characterized by two
distinct binding domains for serine protease. Each domain is comprised of a
beta-hairpin (antiparallel beta-sheet and a cis-proline-containing type VIb
reverse turn) with a short segment making a third strand of antiparallel
beta-sheet. The structure determination and refinement are described, and the
structure is compared to other structures of Bowman-Birk inhibitors as well as
other families of serine protease inhibitors.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.S.Dudkina,
A.A.Selischeva,
and
N.I.Larionova
(2010).
Characteristics of binding of zwitterionic liposomes to water-soluble proteins.
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Biochemistry (Mosc),
75,
224-232.
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K.Prymula,
K.Sałapa,
and
I.Roterman
(2010).
"Fuzzy oil drop" model applied to individual small proteins built of 70 amino acids.
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J Mol Model,
16,
1269-1282.
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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.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
1087-1090.
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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.
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Biophys J,
92,
1638-1650.
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PDB code:
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E.M.Ragg,
V.Galbusera,
A.Scarafoni,
A.Negri,
G.Tedeschi,
A.Consonni,
F.Sessa,
and
M.Duranti
(2006).
Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds.
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FEBS J,
273,
4024-4039.
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PDB code:
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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.
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Acta Biochim Biophys Sin (Shanghai),
37,
283-292.
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P.Kumar,
A.G.Rao,
S.Hariharaputran,
N.Chandra,
and
L.R.Gowda
(2004).
Molecular mechanism of dimerization of Bowman-Birk inhibitors. Pivotal role of ASP76 in the dimerzation.
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J Biol Chem,
279,
30425-30432.
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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.
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Acta Crystallogr D Biol Crystallogr,
59,
1828-1830.
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U.C.Marx,
M.L.Korsinczky,
H.J.Schirra,
A.Jones,
B.Condie,
L.Otvos,
and
D.J.Craik
(2003).
Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide.
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J Biol Chem,
278,
21782-21789.
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PDB codes:
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A.B.Brauer,
G.J.Domingo,
R.M.Cooke,
S.J.Matthews,
and
R.J.Leatherbarrow
(2002).
A conserved cis peptide bond is necessary for the activity of Bowman-Birk inhibitor protein.
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Biochemistry,
41,
10608-10615.
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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.
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Biopolymers,
66,
79-92.
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K.Hatano,
Y.Sawano,
and
M.Tanokura
(2002).
Structure-function relationship of bromelain isoinhibitors from pineapple stem.
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Biol Chem,
383,
1151-1156.
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Y.Sawano,
T.Muramatsu,
K.Hatano,
K.Nagata,
and
M.Tanokura
(2002).
Characterization of genomic sequence coding for bromelain inhibitors in pineapple and expression of its recombinant isoform.
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J Biol Chem,
277,
28222-28227.
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Z.Gáspári,
A.Patthy,
L.Gráf,
and
A.Perczel
(2002).
Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria.
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Eur J Biochem,
269,
527-537.
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PDB codes:
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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.
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Biopolymers,
58,
138-151.
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G.Zhu,
Q.Huang,
Y.Zhu,
Y.Li,
C.Chi,
and
Y.Tang
(2001).
X-Ray study on an artificial mung bean inhibitor complex with bovine beta-trypsin in neat cyclohexane.
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Biochim Biophys Acta,
1546,
98.
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PDB code:
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T.Cierpicki,
J.Bania,
and
J.Otlewski
(2000).
NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
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Protein Sci,
9,
976-984.
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PDB code:
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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.
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Proteins,
35,
321-331.
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PDB code:
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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.
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Acta Crystallogr D Biol Crystallogr,
55,
1920-1922.
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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.
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Acta Crystallogr D Biol Crystallogr,
55,
1244-1246.
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H.K.Song,
and
S.W.Suh
(1998).
Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds.
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Acta Crystallogr D Biol Crystallogr,
54,
441-443.
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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.
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J Protein Chem,
15,
591-598.
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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.
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Eur J Biochem,
242,
122-131.
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PDB code:
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P.Flecker
(1995).
Template-directed protein folding into a metastable state of increased activity.
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Eur J Biochem,
232,
528-535.
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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.
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Eur J Biochem,
212,
549-555.
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PDB code:
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W.J.Chazin
(1992).
NMR structures and methodology.
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Curr Opin Biotechnol,
3,
326-332.
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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.
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Links
