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PDBsum entry 2tgp
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Complex (proteinase/inhibitor)
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PDB id
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2tgp
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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 geometry of the reactive site and of the peptide groups in trypsin, Trypsinogen and its complexes with inhibitors
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Authors
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M.Marquart,
J.Walter,
J.Deisenhofer,
W.Bode,
R.Huber.
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Ref.
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Acta Crystallogr ,Sect B, 1983,
39,
480.
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Secondary reference #1
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Title
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The transition of bovine trypsinogen to a trypsin-Like state upon strong ligand binding. Ii. The binding of the pancreatic trypsin inhibitor and of isoleucine-Valine and of sequentially related peptides to trypsinogen and to p-Guanidinobenzoate-Trypsinogen.
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Author
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W.Bode.
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Ref.
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J Mol Biol, 1979,
127,
357-374.
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PubMed id
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Secondary reference #2
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Title
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The transition of bovine trypsinogen to a trypsin-Like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-Pancreatic trypsin inhibitor complex and of its ternary complex with ile-Val at 1.9 a resolution.
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Authors
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W.Bode,
P.Schwager,
R.Huber.
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Ref.
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J Mol Biol, 1978,
118,
99.
[DOI no: ]
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PubMed id
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Figure 2.
FIG. 2. (a) and (b) Consecutive sections from 8 to 25 through the gPI-TgP difference %`ourier
map. Contours are drawn a8 in Fig. 1. The atomic positions me those of the TP model.
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Figure 4.
FIG. 4. Relative weights of C'' etoms plotted `uemua the amino acid sequence numbers. ( ) TgP;
( I ) TP (for autolysis loop only); (-) TgPI (for autolysis loop only).
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #3
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Title
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Structural basis of the activation and action of trypsin
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Authors
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R.Huber,
W.Bode.
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Ref.
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Acc Chem Res, 1978,
11,
114.
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Secondary reference #4
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Title
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The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor III. Structure of the anhydro-Trypsin-Inhibitor complex.
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Authors
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R.Huber,
W.Bode,
D.Kukla,
U.Kohl,
C.A.Ryan.
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Ref.
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Biophys Struct Mech, 1975,
1,
189-201.
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PubMed id
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Secondary reference #5
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Title
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Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Ii. Crystallographic refinement at 1.9 a resolution.
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Authors
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R.Huber,
D.Kukla,
W.Bode,
P.Schwager,
K.Bartels,
J.Deisenhofer,
W.Steigemann.
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Ref.
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J Mol Biol, 1974,
89,
73.
[DOI no: ]
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PubMed id
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Figure 2.
FIG. 2. Final difference Fourier mp at Tyr 69. Contours from O-1 e/A3 in 0.06 e/A3 steps. Solid
lines indicate positive, broken lines negative residual density.
The aromaic ring is mobile rotating around 2'.
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Figure 7.
FI. 7. Lys 15 (I) amide.
The Lys 15 (I) 0 is -34'' out of the plane formed by 0, C, N. It is strongly deformed towards
a tetrahedral carbon. Ala 16 (I) Cfl is in the upper right-hand corner.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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