1r1j: Difference between revisions
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[[Image:1r1j.gif|left|200px]] | [[Image:1r1j.gif|left|200px]] | ||
'''STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS''' | {{Structure | ||
|PDB= 1r1j |SIZE=350|CAPTION= <scene name='initialview01'>1r1j</scene>, resolution 2.35Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=OIR:N-(3-PHENYL-2-SULFANYLPROPANOYL)PHENYLALANYLALANINE'>OIR</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Neprilysin Neprilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.11 3.4.24.11] | |||
|GENE= MME, EPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1R1J is a [ | 1R1J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1J OCA]. | ||
==Reference== | ==Reference== | ||
Structural analysis of neprilysin with various specific and potent inhibitors., Oefner C, Roques BP, Fournie-Zaluski MC, Dale GE, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):392-6. Epub 2004, Jan 23. PMID:[http:// | Structural analysis of neprilysin with various specific and potent inhibitors., Oefner C, Roques BP, Fournie-Zaluski MC, Dale GE, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):392-6. Epub 2004, Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14747736 14747736] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Neprilysin]] | [[Category: Neprilysin]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:45:37 2008'' |
Revision as of 14:45, 20 March 2008
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, resolution 2.35Å | |||||||
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Ligands: | , and | ||||||
Gene: | MME, EPN (Homo sapiens) | ||||||
Activity: | Neprilysin, with EC number 3.4.24.11 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT INHIBITORS
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Membranous glomerulonephritis, antenatal OMIM:[120520], Neutral endopeptidase deficiency OMIM:[120520], Schizophrenia, susceptibility to OMIM:[607265]
About this StructureAbout this Structure
1R1J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural analysis of neprilysin with various specific and potent inhibitors., Oefner C, Roques BP, Fournie-Zaluski MC, Dale GE, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):392-6. Epub 2004, Jan 23. PMID:14747736
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