1dl9: Difference between revisions
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<StructureSection load='1dl9' size='340' side='right'caption='[[1dl9]]' scene=''> | <StructureSection load='1dl9' size='340' side='right'caption='[[1dl9]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <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'>[ | </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> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Latest revision as of 14:07, 28 July 2021
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THREE-DIMENSIONAL CONSTRUCTION OF THE ACTIVE SITE (REGION 507-749) OF HUMAN NEUTRAL ENDOPEPTIDASE (EC.3.4.24.11)THREE-DIMENSIONAL CONSTRUCTION OF THE ACTIVE SITE (REGION 507-749) OF HUMAN NEUTRAL ENDOPEPTIDASE (EC.3.4.24.11)
Structural highlights
Publication Abstract from PubMedA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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