2yb9 | pdb_00002yb9

Crystal Structure of Human Neutral Endopeptidase complexed with a heteroarylalanine diacid.

spinqualitylabelsall models 2yb9, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yb9 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: HA0, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NEP_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. Publication Abstract from PubMed Heteroarylalanine 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neprilysin

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