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1brb
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(New page: 200px<br /><applet load="1brb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1brb, resolution 2.1Å" /> '''CRYSTAL STRUCTURES OF...)
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Revision as of 09:44, 20 November 2007
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CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI
Overview
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.
About this Structure
1BRB is a Protein complex structure of sequences from Rattus norvegicus. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI., Perona JJ, Tsu CA, Craik CS, Fletterick RJ, J Mol Biol. 1993 Apr 5;230(3):919-33. PMID:7683059
Page seeded by OCA on Tue Nov 20 11:51:16 2007
