1BRB

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

1BRB の概要

• エントリーDOI: 10.2210/pdb1brb/pdb
• 分子名称: TRYPSIN, PANCREATIC TRYPSIN INHIBITOR (3 entities in total)
• 機能のキーワード: complex(proteinase-inhibitor), complex(proteinase-inhibitor) complex, complex(proteinase/inhibitor)
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Secreted, extracellular space: P00763; Secreted: P00974
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30222.17

構造登録者

Perona, J.J.,Fletterick, R.J. (登録日: 1992-12-17, 公開日: 1994-07-31, 最終更新日: 2024-10-16)

主引用文献

Perona, J.J.,Tsu, C.A.,Craik, C.S.,Fletterick, R.J.
Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI.
J.Mol.Biol., 230:919-933, 1993

PubMed 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.

PubMed: 7683059
DOI: 10.1006/jmbi.1993.1210

実験手法

X-RAY DIFFRACTION (2.1 Å)