 |
PDBsum entry 1brb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Complex(proteinase/inhibitor)
|
PDB id
|
|
|
|
1brb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structures of rat anionic trypsin complexed with the protein inhibitors appi and bpti.
|
|
|
Authors
|
|
J.J.Perona,
C.A.Tsu,
C.S.Craik,
R.J.Fletterick.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
230,
919-933.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The crystal structure of rat anionic trypsin D189G/G226D has been determined in
complexes with each of the protein inhibitors APPI (amyloid beta-protein
precursor inhibitor domain) and BPTI (bovine pancreatic trypsin inhibitor) at
resolutions of 2.5 A and 2.1 A, respectively. Comparisons with the structure of
the bovine trypsin-BPTI complex show that the enzyme-inhibitor interactions in
rat trypsin are dominated to a much greater degree by attractive and repulsive
electrostatic forces. Decreased structural complementarity in the flanking
regions of the interface formed with BPTI is reflected in significantly weaker
inhibition relative to bovine trypsin. The primary active site loop of BPTI
adopts slightly different conformations when bound to rat and cow trypsins,
reflecting a broader entrance to the binding pocket in the former. Tight
complementarity of each loop conformer to the respective active sites then gives
rise to significantly different overall orientations of the inhibitor when bound
to the two enzymes. The crystal structures of trypsin bound to these protein
inhibitors are excellent models of the Michaelis complexes, which permit
visualization of substrate interactions both N and C-terminal to the cleaved
bond, while maintaining identical reaction chemistry. They will be uniquely
useful to the structure-function analysis of variant rat trypsin enzymes.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Relocating a negative charge in the binding pocket of trypsin.
|
|
|
Authors
|
|
J.J.Perona,
C.A.Tsu,
M.E.Mcgrath,
C.S.Craik,
R.J.Fletterick.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
230,
934-949.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
