2yb9
From Proteopedia
Crystal Structure of Human Neutral Endopeptidase complexed with a heteroarylalanine diacid.
Structural highlights
FunctionNEP_HUMAN Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.[1] [2] [3] Publication Abstract from PubMedHeteroarylalanine derivatives 4 were designed as potential inhibitors of neutral endopeptidase (NEP EC 3.4.24.11). Selectivity over other zinc metalloproteinases was explored through occupation of the S2' subsite within NEP. Structural optimisation led to the identification of 5-phenyl oxazole 4f, a potent and selective NEP inhibitor. A crystal structure of the inhibitor bound complex is reported. Synthesis and evaluation of heteroarylalanine diacids as potent and selective neutral endopeptidase inhibitors.,Glossop MS, Bazin RJ, Dack KN, Fox DN, Macdonald GA, Mills M, Owen DR, Phillips C, Reeves KA, Ringer TJ, Strang RS, Watson CA Bioorg Med Chem Lett. 2011 Jun 1;21(11):3404-6. Epub 2011 Apr 5. PMID:21515054[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Bazin RJ | Dack KN | Done S | Fox DNA | Glossop MS | MacDonald GA | Mills M | Owen DR | Phillips C | Reeves KA | Ringer TJ | Strang RS | Watson CAL
