1r1j: Difference between revisions

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OCA

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-[[Image:1r1j.gif|left|200px]]
+{{Seed}}
+[[Image:1r1j.png|left|200px]]
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 {{STRUCTURE_1r1j|  PDB=1r1j  |  SCENE=  }}
-'''STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS'''
+===STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS===
-==Overview==
+<!--
-Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor. Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents. Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described. The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_14747736}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14747736 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14747736}}
 ==About this Structure==
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 [[Category: Glycoprotein]]
 [[Category: Metalloprotease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:57:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:43:27 2008''