This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1brb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1brb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1brb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1brb| PDB=1brb | SCENE= }}
{{STRUCTURE_1brb| PDB=1brb | SCENE= }}
-
'''CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7683059}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7683059 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7683059}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Fletterick, R J.]]
[[Category: Fletterick, R J.]]
[[Category: Perona, J J.]]
[[Category: Perona, J J.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:51:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:36:11 2008''

Revision as of 16:36, 30 June 2008

Image:1brb.png

Template:STRUCTURE 1brb

CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI

Template:ABSTRACT PUBMED 7683059

About this Structure

1BRB is a Protein complex structure of sequences from Rattus norvegicus. 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 Mon Jun 30 19:36:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1brb"
Personal tools