1dl9
From Proteopedia
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{{Theoretical_model}} | {{Theoretical_model}} | ||
| - | [[ | + | ==THREE-DIMENSIONAL CONSTRUCTION OF THE ACTIVE SITE (REGION 507-749) OF HUMAN NEUTRAL ENDOPEPTIDASE (EC.3.4.24.11)== |
| + | <StructureSection load='1dl9' size='340' side='right'caption='[[1dl9]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DL9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dl9 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1dl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dl9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:10195285</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1dl9" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Theoretical Model]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Antonczak, S]] | [[Category: Antonczak, S]] | ||
[[Category: Fournie-, M C]] | [[Category: Fournie-, M C]] | ||
Current revision
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THREE-DIMENSIONAL CONSTRUCTION OF THE ACTIVE SITE (REGION 507-749) OF HUMAN NEUTRAL ENDOPEPTIDASE (EC.3.4.24.11)
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