1itu
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(New page: 200px<br /> <applet load="1itu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1itu, resolution 2.00Å" /> '''HUMAN RENAL DIPEPTI...)
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Revision as of 15:28, 12 November 2007
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HUMAN RENAL DIPEPTIDASE COMPLEXED WITH CILASTATIN
Contents |
Overview
Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing, dipeptides and is involved in hydrolytic metabolism of penem and, carbapenem beta-lactam antibiotics. The crystal structures of the, saccharide-trimmed enzyme are determined as unliganded and, inhibitor-liganded forms. They are informative for designing new, antibiotics that are not hydrolyzed by this enzyme. The active site in, each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is, composed of binuclear zinc ions bridged by the Glu125 side-chain located, at the bottom of the barrel, and it faces toward the microvillar membrane, of a kidney tubule. A dipeptidyl moiety of the therapeutically used, cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The, barrel and active-site architectures utilizing catalytic metal ions, exhibit unexpected similarities to those of the murine adenosine deaminase, and the catalytic domain of the bacterial urease.
Disease
Known disease associated with this structure: Dystonia-12 OMIM:[182350]
About this Structure
1ITU is a Single protein structure of sequence from Homo sapiens with NAG, ZN and CIL as ligands. Active as Membrane dipeptidase, with EC number 3.4.13.19 Full crystallographic information is available from OCA.
Reference
Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis., Nitanai Y, Satow Y, Adachi H, Tsujimoto M, J Mol Biol. 2002 Aug 9;321(2):177-84. PMID:12144777
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