2iul

Revision as of 18:55, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2iul" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iul, resolution 2.01Å" /> '''HUMAN TACE G13 MUTA...)
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HUMAN TACE G13 MUTANT

File:2iul.gif


2iul, resolution 2.01Å

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OverviewOverview

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 StructureAbout this Structure

2IUL is a [Single protein] structure of sequence from [Homo sapiens] with NAG, ACT, CL and ZN as [ligands]. Full crystallographic information is available from [OCA].

ReferenceReference

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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