7EST

Interaction of the peptide CF3-LEU-ALA-NH-C6H4-CF3(TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 Angstroms

7EST の概要

• エントリーDOI: 10.2210/pdb7est/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000366
• 分子名称: ELASTASE, N-(trifluoroacetyl)-L-leucyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: serine proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26871.01

構造登録者

Li De Lasierra, I.,Prange, T. (登録日: 1990-06-15, 公開日: 1991-10-15, 最終更新日: 2024-10-30)

主引用文献

de la Sierra, I.L.,Papamichael, E.,Sakarellos, C.,Dimicoli, J.L.,Prange, T.
Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A.
J.Mol.Recog., 3:36-44, 1990

PubMed Abstract: The peptide trifluoroacetyl-Leu-Ala-(p-trifluoromethylanilide), is a reversible inhibitor of pancreatic porcine elastase and is characterized by a Km of 2.5 x 10(-8) M. Co-crystals of the 1:1 complex were obtained in an acetate buffer + dimethylformamide solution at pH 5.7. Diffraction data were recorded on films at the LURE synchrotron facility. The inhibitor was localized on difference Fourier maps, and the refinement of the structure was performed by simulated annealing (XPLOR). The current agreement factor is R = 19% (for 13224 observed structure factors and 1.8 A effective resolution). The RMS deviations from ideality of bond distances and angles are 0.02 A and 2 degrees, respectively. The inhibitor molecule was found in the active site, bent around the side chain of Phe-215 in a geometry that resembles the previously reported structure of the CF3-Lys-Ala complex at 2.5 A, in a parallel beta-sheet association with the loop 214-216. The analysis of the close contacts (less than 3.5 A) indicates that the trifluoromethylamide bond interacts with the active site and not the Leu-Ala or Ala-anilide bonds. The two fluorinated groups of the inhibitor exhibit different specificities: the trifluoroacetyl group (N terminus) is tightly stacked between the two chain loops 191-195 and 213-215, while the trifluoromethylanilide (C terminus) shows less specificity and only a single contact.

PubMed: 2354062
DOI: 10.1002/jmr.300030104

実験手法

X-RAY DIFFRACTION (1.8 Å)