2iux

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2iux, resolution 2.8Å

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HUMAN TACE MUTANT G1234

Overview

Human angiotensin-converting enzyme is an important drug target for which, little structural information has been available until recent years. The, slow progress in obtaining a crystal structure was due to the problem of, surface glycosylation, a difficulty that has thus far been overcome by the, use of a glucosidase-1 inhibitor in the tissue culture medium. However, the prohibitive cost of these inhibitors and incomplete glucosidase, inhibition makes alternative routes to minimizing the N-glycan, heterogeneity desirable. Here, glycosylation in the testis isoform (tACE), has been reduced by Asn-Gln point mutations at N-glycosylation sites, and, the crystal structures of mutants having two and four intact sites have, been solved to 2.0 A and 2.8 A, respectively. Both mutants show close, ... [(full description)]

About this Structure

2IUX is a [Single protein] structure of sequence from [Homo sapiens] with NAG, ACT, ZN, CL and NXA as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure of testis ACE glycosylation mutants and evidence for conserved domain movement., Watermeyer JM, Sewell BT, Schwager SL, Natesh R, Corradi HR, Acharya KR, Sturrock ED, Biochemistry. 2006 Oct 24;45(42):12654-63. PMID:17042482

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