1eld
From Proteopedia
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STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS
Overview
The X-ray crystal structures of two new (trifluoroacetyl)dipeptide, p-(trifluoromethyl)anilide (TFA-dipeptide-TFM) inhibitors complexed to, porcine pancreatic elastase are presented. TFA-Val-Ala-TFM and, TFA-Phe-Ala-TFM both bind to elastase with the TFA group in the S1, subsite, Val or Phe in the S2 subsite, Ala in the S3 subsite, and the TFM, group in the S4 subsite. Five other TFA-dipeptide-anilide/elastase crystal, structures are available (two TFA-X-Ala-p-(trifluoromethyl)anilide, X =, Lys, Leu, and three TFA-Lys-X-p-isopropylanilide, X = Pro, Leu, Phe). The, four inhibitors with the trifluoromethyl substituent on the anilide ring, bind in a single mode to elastase, whereas superposition of the three, inhibitors with the isopropyl substituent on the anilide ring show three, different modes of binding to the protein [Mattos, C., et al. (1994), Nature Struct. Biol. 1, 55-58]. The seven structures are taken together in, a detailed analysis of the active site of porcine pancreatic elastase. The, inhibition constants for the inhibitors are used in combination with the, crystal structures to understand the specificity of the different elastase, subsites.
About this Structure
1ELD is a Single protein structure of sequence from Sus scrofa with CA, TFA and ACY as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.
Reference
Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors., Mattos C, Giammona DA, Petsko GA, Ringe D, Biochemistry. 1995 Mar 14;34(10):3193-203. PMID:7880814
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