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PDBsum entry 1bea
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Serine protease inhibitor
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PDB id
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1bea
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
37:15277-15288
(1998)
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PubMed id:
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Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution.
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C.A.Behnke,
V.C.Yee,
I.L.Trong,
L.C.Pedersen,
R.E.Stenkamp,
S.S.Kim,
G.R.Reeck,
D.C.Teller.
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ABSTRACT
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Corn Hageman factor inhibitor (CHFI) is a bifunctional 127 residue, 13.6 kDa
protein isolated from corn seeds. It inhibits mammalian trypsin and Factor XIIa
(Hageman Factor) of the contact pathway of coagulation as well as alpha-amylases
from several insect species. Among the plasma proteinases, CHFI specifically
inhibits Factor XIIa without affecting the activity of other coagulation
proteinases. We have isolated CHFI from corn and determined the crystallographic
structure at 1.95 A resolution. Additionally, we have solved the structure of
the recombinant protein produced in Escherichia coli at 2.2 A resolution. The
two proteins are essentially identical. The proteinase binding loop is in the
canonical conformation for proteinase inhibitors. In an effort to understand
alpha-amylase inhibition by members of the family of 25 cereal
trypsin/alpha-amylase inhibitors, we have made three-dimensional models of
several proteins in the family based on the CHFI coordinates and the coordinates
determined for wheat alpha-amylase inhibitor 0.19 [Oda, Y., Matsunaga, T.,
Fukuyama, K., Miyazaki, T., and Morimoto, T. (1997) Biochemistry 36,
13503-13511]. From an analysis of the models and a structure-based sequence
analysis, we propose a testable hypothesis for the regions of these proteins
which bind alpha-amylase. In the course of the investigations, we have found
that the cereal trypsin/alpha-amylase inhibitor family is evolutionarily related
to the family of nonspecific lipid-transfer proteins of plants. This is a new
addition to the group which now consists of the trypsin/alpha-amylase
inhibitors, 2S seed storage albumins, and the lipid-transfer family. Apparently,
the four-helix conformation has been a successful vehicle in plant evolution for
providing protection from predators, food for the embryo, and lipid transfer.
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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.Buehler,
L.Urzhumtseva,
V.Y.Lunin,
and
A.Urzhumtsev
(2009).
Cluster analysis for phasing with molecular replacement: a feasibility study.
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Acta Crystallogr D Biol Crystallogr,
65,
644-650.
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J.T.Christeller
(2005).
Evolutionary mechanisms acting on proteinase inhibitor variability.
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FEBS J,
272,
5710-5722.
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I.T.Campos,
B.G.Guimarães,
F.J.Medrano,
A.S.Tanaka,
and
J.A.Barbosa
(2004).
Crystallization, data collection and phasing of infestin 4, a factor XIIa inhibitor.
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Acta Crystallogr D Biol Crystallogr,
60,
2051-2053.
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L.Urzhumtseva,
N.Lunina,
A.Fokine,
J.P.Samama,
V.Y.Lunin,
and
A.Urzhumtsev
(2004).
Ab initio phasing based on topological restraints: automated determination of the space group and the number of molecules in the unit cell.
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Acta Crystallogr D Biol Crystallogr,
60,
1519-1526.
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Z.Wu,
A.Hasan,
T.Liu,
D.C.Teller,
and
J.W.Crabb
(2004).
Identification of CRALBP ligand interactions by photoaffinity labeling, hydrogen/deuterium exchange, and structural modeling.
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J Biol Chem,
279,
27357-27364.
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R.Cazalis,
T.Aussenac,
L.Rhazi,
A.Marin,
and
J.F.Gibrat
(2003).
Homology modeling and molecular dynamics simulations of the N-terminal domain of wheat high molecular weight glutenin subunit 10.
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Protein Sci,
12,
34-43.
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A.Urzhumtsev,
and
L.Urzhumtseva
(2002).
Multiple rotation function.
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Acta Crystallogr D Biol Crystallogr,
58,
2066-2075.
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O.L.Franco,
D.J.Rigden,
F.R.Melo,
and
M.F.Grossi-De-Sá
(2002).
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
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Eur J Biochem,
269,
397-412.
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C.P.Selitrennikoff
(2001).
Antifungal proteins.
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Appl Environ Microbiol,
67,
2883-2894.
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Y.W.Chen
(2001).
Solution solution: using NMR models for molecular replacement.
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Acta Crystallogr D Biol Crystallogr,
57,
1457-1461.
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S.Gourinath,
N.Alam,
A.Srinivasan,
C.Betzel,
and
T.P.Singh
(2000).
Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution.
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Acta Crystallogr D Biol Crystallogr,
56,
287-293.
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PDB code:
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Y.W.Chen,
E.J.Dodson,
and
G.J.Kleywegt
(2000).
Does NMR mean "not for molecular replacement"? Using NMR-based search models to solve protein crystal structures.
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Structure,
8,
R213-R220.
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P.J.Pereira,
V.Lozanov,
A.Patthy,
R.Huber,
W.Bode,
S.Pongor,
and
S.Strobl
(1999).
Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution.
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Structure,
7,
1079-1088.
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PDB code:
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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
