7est
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:7est.gif|left|200px]] | [[Image:7est.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_7est", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_7est| PDB=7est | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 ANGSTROMS''' | '''INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 ANGSTROMS''' | ||
| Line 28: | Line 25: | ||
[[Category: Lasierra, I Li De.]] | [[Category: Lasierra, I Li De.]] | ||
[[Category: Prange, T.]] | [[Category: Prange, T.]] | ||
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:44:36 2008'' | |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:44, 4 May 2008
INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 ANGSTROMS
Overview
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.
About this Structure
7EST is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A., de la Sierra IL, Papamichael E, Sakarellos C, Dimicoli JL, Prange T, J Mol Recognit. 1990 Feb;3(1):36-44. PMID:2354062 Page seeded by OCA on Sun May 4 22:44:36 2008
