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1itq
From Proteopedia
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[[Image:1itq.jpg|left|200px]] | [[Image:1itq.jpg|left|200px]] | ||
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'''HUMAN RENAL DIPEPTIDASE''' | '''HUMAN RENAL DIPEPTIDASE''' | ||
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[[Category: Satow, Y.]] | [[Category: Satow, Y.]] | ||
[[Category: Tsujimoto, M.]] | [[Category: Tsujimoto, M.]] | ||
| - | [[Category: | + | [[Category: Cilastatin]] |
| - | [[Category: | + | [[Category: Dipeptidase]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Membrane-bound]] |
| - | + | [[Category: Zinc protease beta-lactamase]] | |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:24:09 2008'' |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:24, 2 May 2008
HUMAN RENAL DIPEPTIDASE
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.
About this Structure
1ITQ is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Fri May 2 20:24:09 2008
