3dwb | pdb_00003dwb

structure of human ECE-1 complexed with phosphoramidon

spinqualitylabelsall models 3dwb, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dwb is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 5HD, RDF, ZN Related: 1dmt Gene: ECE1 (HUMAN) Activity: Endothelin-converting enzyme 1, with EC number 3.4.24.71 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [ECE1_HUMAN] Defects in ECE1 are a cause of Hirschsprung disease cardiac defects and autonomic dysfunction (HSCRCDAD) [MIM:613870]. It is a form of Hirschsprung disease with skip-lesions defects, craniofacial abnormalities and other dysmorphic features, and autonomic dysfunction. Function [ECE1_HUMAN] Converts big endothelin-1 to endothelin-1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Endothelin-converting enzyme I (ECE-1) is a mammalian type II integral membrane zinc-containing endopeptidase. ECE-1 catalyzes the final step in the biosynthesis of endothelins in a rate-limiting fashion, through post-translational conversion of the biologically inactive big endothelins. Endothelin-1 overproduction has been implicated in a heterogeneous list of diseases including systemic and pulmonary hypertension, stroke and asthma, cardiac and renal failure. Therefore, ECE-1 is a prime therapeutic target for the regulation of endothelin-1 production in vivo and there is considerable interest in selective inhibitors of this enzyme. Here, we present the crystal structure of the extracellular domain (residues 90-770) of human ECE-1 (C428S) with the generic metalloprotease inhibitor phosphoramidon determined at 2.38 A resolution. The structure is closely related to that of human NEP, providing essential information for a detailed understanding of ligand-binding, specificity determinants as well as selectivity criteria. Selective inhibitors of ECE-1s should have beneficial effects for the treatment of diseases in which an overproduction of ETs plays a pathogenic role. Structure of human endothelin-converting enzyme I complexed with phosphoramidon.,Schulz H, Dale GE, Karimi-Nejad Y, Oefner C J Mol Biol. 2009 Jan 9;385(1):178-87. Epub 2008 Nov 1. PMID:18992253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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