6est

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6est, resolution 1.8Å

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INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 ANGSTROMS

OverviewOverview

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 StructureAbout this Structure

6EST is a Single protein structure of sequence from Sus scrofa with CA, SO4 and DMF as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.

ReferenceReference

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

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