1brb

<StructureSection load='1brb' size='340' side='right' caption='[[1brb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1brb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BRB FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1brb RCSB], [http://www.ebi.ac.uk/pdbsum/1brb PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brb_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:7683059</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Basic Pancreatic Trypsin Inhibitor|Basic Pancreatic Trypsin Inhibitor]]

*[[Trypsin|Trypsin]]

[[Category: Fletterick, R J]]

[[Category: Perona, J J]]