1dl9 | pdb_00001dl9

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THREE-DIMENSIONAL CONSTRUCTION OF THE ACTIVE SITE (REGION 507-749) OF HUMAN NEUTRAL ENDOPEPTIDASE (EC.3.4.24.11)

spinqualitylabelsall models 1dl9 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A three-dimensional model of the 507-749 region of neutral endopeptidase-24.11 (NEP; E.C.3.4.24.11) was constructed integrating the results of secondary structure predictions and sequence homologies with the bacterial endopeptidase thermolysin. Additional data were extracted from the structure of two other metalloproteases, astacin and stromelysin. The resulting model accounts for the main biological properties of NEP and has been used to describe the environment close to the zinc atom defining the catalytic site. The analysis of several thiol inhibitors, complexed in the model active site, revealed the presence of a large hydrophobic pocket at the S1' subsite level. This is supported by the nature of the constitutive amino acids. The computed energies of bound inhibitors correspond with the relative affinities of the stereoisomers of benzofused macrocycle derivatives of thiorphan. The model could be used to facilitate the design of new NEP inhibitors, as illustrated in the paper. A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC.3.4.24.11).,Tiraboschi G, Jullian N, Thery V, Antonczak S, Fournie-Zaluski MC, Roques BP Protein Eng. 1999 Feb;12(2):141-9. PMID:10195285 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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