1itq: Difference between revisions

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[[Image:1itq.jpg|left|200px]]
{{Seed}}
[[Image:1itq.png|left|200px]]


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{{STRUCTURE_1itq|  PDB=1itq  |  SCENE=  }}  
{{STRUCTURE_1itq|  PDB=1itq  |  SCENE=  }}  


'''HUMAN RENAL DIPEPTIDASE'''
===HUMAN RENAL DIPEPTIDASE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12144777}}


==About this Structure==
==About this Structure==
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[[Category: Membrane-bound]]
[[Category: Membrane-bound]]
[[Category: Zinc protease beta-lactamase]]
[[Category: Zinc protease beta-lactamase]]
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Revision as of 10:59, 1 July 2008

File:1itq.png

Template:STRUCTURE 1itq

HUMAN RENAL DIPEPTIDASE

Template:ABSTRACT PUBMED 12144777

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

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