1itq: Difference between revisions

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[[Image:1itq.jpg|left|200px]]
[[Image:1itq.jpg|left|200px]]


{{Structure
<!--
|PDB= 1itq |SIZE=350|CAPTION= <scene name='initialview01'>1itq</scene>, resolution 2.30&Aring;
The line below this paragraph, containing "STRUCTURE_1itq", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_dipeptidase Membrane dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.19 3.4.13.19] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1itq| PDB=1itq  | SCENE= }}  
|RELATEDENTRY=[[1itu|1ITU]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1itq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1itq OCA], [http://www.ebi.ac.uk/pdbsum/1itq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1itq RCSB]</span>
}}


'''HUMAN RENAL DIPEPTIDASE'''
'''HUMAN RENAL DIPEPTIDASE'''
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[[Category: Satow, Y.]]
[[Category: Satow, Y.]]
[[Category: Tsujimoto, M.]]
[[Category: Tsujimoto, M.]]
[[Category: cilastatin]]
[[Category: Cilastatin]]
[[Category: complex (hydrolase/inhibitor)]]
[[Category: Dipeptidase]]
[[Category: dipeptidase]]
[[Category: Glycoprotein]]
[[Category: glycoprotein]]
[[Category: Membrane-bound]]
[[Category: membrane-bound]]
[[Category: Zinc protease beta-lactamase]]
[[Category: zinc protease beta-lactamase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:24:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:24:34 2008''

Revision as of 17:24, 2 May 2008

File:1itq.jpg

Template:STRUCTURE 1itq

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

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