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PDBsum entry 4tpi
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Hydrolase/hydrolase inhibitor
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PDB id
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4tpi
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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 2.2-A (0.22-Nm) X-Ray crystal structure of the ternary complex formed by bovine trypsinogen, Valine-Valine and the arg15 analogue of bovine pancreatic trypsin inhibitor.
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Authors
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W.Bode,
J.Walter,
R.Huber,
H.R.Wenzel,
H.Tschesche.
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Ref.
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Eur J Biochem, 1984,
144,
185-190.
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PubMed id
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Abstract
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Large orthorhombic crystals of the complex formed by bovine trypsinogen and a
semisynthetic homologous bovine pancreatic trypsin inhibitor with the
reactive-site lysine residue replaced by an arginine residue [( Arg15]PTI) have
been obtained which are isomorphous with the crystals of PTI-trypsinogen [Bode,
W., Schwager, P. and Huber, R. (1978) J. Mol. Biol. 118, 99-112]. The X-ray
crystal structure of the ternary complex of trypsinogen-[Arg15]PTI with the
dipeptide Val-Val has been determined by X-ray data to 2.2-A (0.22-nm)
resolution by means of difference Fourier methods and has been
crystallographically refined to a final R-value of 0.17. Replacement of the
reactive-site Lys15 by an arginine residue is accompanied in the complex by
small movements of polar side groups of trypsin and enclosed solvent molecules
within the specificity pocket. Only solvent molecule 414 OH which mediates the
hydrogen bond interactions between Lys15 NZ and Asp189 carboxylate is expelled,
thus allowing the bulkier guanidyl group to approach this carboxylate. The
dipeptide Val-Val binds in the pocket accepting the Ile-Val N-terminus in
trypsin. The cavity left by the CD-methyl group of Ile16 upon replacement by a
valine residue is only partially filled by slight rearrangements of neighbouring
peptide side chains. Part of the positive free energy change observed upon
replacement of Ile-Val may allow for the maintenance of this cavity.
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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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