4TPI

THE REFINED 2.2-ANGSTROMS (0.22-NM) X-RAY CRYSTAL STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOGUE OF BOVINE PANCREATIC TRYPSIN INHIBITOR

4TPI の概要

• エントリーDOI: 10.2210/pdb4tpi/pdb
• 分子名称: TRYPSINOGEN, BOVINE PANCREATIC TRYPSIN INHIBITOR, VALINE, ... (6 entities in total)
• 機能のキーワード: complex (proteinase-inhibitor), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted, extracellular space: P00760; Secreted: P00974
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31035.03

構造登録者

Bode, W.,Walter, J. (登録日: 1985-06-11, 公開日: 1985-11-08, 最終更新日: 2024-10-23)

主引用文献

Bode, W.,Walter, J.,Huber, R.,Wenzel, H.R.,Tschesche, H.
The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor
Eur.J.Biochem., 144:185-190, 1984

PubMed Abstract: Large orthorhombic crystals of the complex formed by bovine trypsinogen and a semisynthetic homologous bovine pancreatic trypsin inhibitor with the reactive-site lysine residue replaced by an arginine residue [( Arg15]PTI) have been obtained which are isomorphous with the crystals of PTI-trypsinogen [Bode, W., Schwager, P. and Huber, R. (1978) J. Mol. Biol. 118, 99-112]. The X-ray crystal structure of the ternary complex of trypsinogen-[Arg15]PTI with the dipeptide Val-Val has been determined by X-ray data to 2.2-A (0.22-nm) resolution by means of difference Fourier methods and has been crystallographically refined to a final R-value of 0.17. Replacement of the reactive-site Lys15 by an arginine residue is accompanied in the complex by small movements of polar side groups of trypsin and enclosed solvent molecules within the specificity pocket. Only solvent molecule 414 OH which mediates the hydrogen bond interactions between Lys15 NZ and Asp189 carboxylate is expelled, thus allowing the bulkier guanidyl group to approach this carboxylate. The dipeptide Val-Val binds in the pocket accepting the Ile-Val N-terminus in trypsin. The cavity left by the CD-methyl group of Ile16 upon replacement by a valine residue is only partially filled by slight rearrangements of neighbouring peptide side chains. Part of the positive free energy change observed upon replacement of Ile-Val may allow for the maintenance of this cavity.

PubMed: 6207021
DOI: 10.1111/j.1432-1033.1984.tb08447.x

実験手法

X-RAY DIFFRACTION (2.2 Å)