1brb: Difference between revisions
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<StructureSection load='1brb' size='340' side='right' caption='[[1brb]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1brb' size='340' side='right' caption='[[1brb]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1brb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1brb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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> | </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> | <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://pdbe.org/1brb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1brb RCSB], [http://www.ebi.ac.uk/pdbsum/1brb PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1brb" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Fletterick, R J]] | [[Category: Fletterick, R J]] | ||
[[Category: Perona, J J]] | [[Category: Perona, J J]] | ||
Revision as of 10:57, 11 September 2015
CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTICRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI
Structural highlights
Function[BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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