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PDBsum entry 1ppe
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Hydrolase/hydrolase inhibitor
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PDB id
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1ppe
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The refined 2.0 a X-Ray crystal structure of the complex formed between bovine beta-Trypsin and cmti-I, A trypsin inhibitor from squash seeds (cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase a inhibitor from potatoes.
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Authors
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W.Bode,
H.J.Greyling,
R.Huber,
J.Otlewski,
T.Wilusz.
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Ref.
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Febs Lett, 1989,
242,
285-292.
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PubMed id
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Abstract
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The stoichiometric complex formed between bovine beta-trypsin and the Cucurbita
maxima trypsin inhibitor I (CMTI-I) was crystallized and its X-ray crystal
structure determined using Patterson search techniques. Its structure has been
crystallographically refined to a final R value of 0.152 (6.0-2.0 A). CMTI-I is
of ellipsoidal shape; it lacks helices or beta-sheets, but consists of turns and
connecting short polypeptide stretches. The disulfide pairing is CYS-3I-20I,
Cys-10I-22I and Cys-16I-28I. According to the polypeptide fold and disulfide
connectivity its structure resembles that of the carboxypeptidase A inhibitor
from potatoes. Thirteen of the 29 inhibitor residues are in direct contact with
trypsin; most of them are in the primary binding segment Val-2I (P4)-Glu-9I
(P4') which contains the reactive site bond Arg-5I-Ile-6I and is in a
conformation observed also for other serine proteinase inhibitors.
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Secondary reference #1
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Title
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Ligand binding: proteinase-Protein inhibitor interactions
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Authors
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W.Bode,
R.Huber.
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Ref.
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curr opin struct biol, 1991,
1,
45.
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Secondary reference #2
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Title
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Nuclear magnetic resonance solution and X-Ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop.
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Authors
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T.A.Holak,
W.Bode,
R.Huber,
J.Otlewski,
T.Wilusz.
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Ref.
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J Mol Biol, 1989,
210,
649-654.
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PubMed id
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Secondary reference #3
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Title
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The squash family of serine proteinase inhibitors. Amino acid sequences and association equilibrium constants of inhibitors from squash, Summer squash, Zucchini, And cucumber seeds.
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Authors
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M.Wieczorek,
J.Otlewski,
J.Cook,
K.Parks,
J.Leluk,
A.Wilimowska-Pelc,
A.Polanowski,
T.Wilusz,
M.Laskowski.
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Ref.
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Biochem Biophys Res Commun, 1985,
126,
646-652.
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PubMed id
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Secondary reference #4
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Title
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Amino-Acid sequence of two trypsin isoinhibitors, Itd i and itd III from squash seeds (cucurbita maxima).
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Authors
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T.Wilusz,
M.Wieczorek,
A.Polanowski,
A.Denton,
J.Cook,
M.Laskowski.
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Ref.
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Hoppe Seylers Z Physiol Chem, 1983,
364,
93-95.
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PubMed id
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Secondary reference #5
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Title
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The refined crystal structure of bovine beta-Trypsin at 1.8 a resolution. Ii. Crystallographic refinement, Calcium binding site, Benzamidine binding site and active site at ph 7.0.
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Authors
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W.Bode,
P.Schwager.
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Ref.
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J Mol Biol, 1975,
98,
693-717.
[DOI no: ]
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PubMed id
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Figure 4.
FiG. 4. Stereo pair of the calcium-bindng loop including the calcium ion and internal water
molecules.
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Figure 7.
Fro. 7. Stereo pair of the region aroun the salt bridge between the benzamidine and Asp189
in benzamidine-inhibited trpsin (a) and side chain of LyslS(I) an Asp189 in he trysin-
inhibitor complex (b), both in complex orientation.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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