1r1o

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[[Image:1r1o.jpg|left|200px]]
 
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==Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase==
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The line below this paragraph, containing "STRUCTURE_1r1o", creates the "Structure Box" on the page.
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<StructureSection load='1r1o' size='340' side='right'caption='[[1r1o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1r1o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1O FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SDC:S-[2-(AMINOSULFONYL)ETHYL]-D-CYSTEINE'>SDC</scene></td></tr>
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{{STRUCTURE_1r1o| PDB=1r1o | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1o OCA], [https://pdbe.org/1r1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1o RCSB], [https://www.ebi.ac.uk/pdbsum/1r1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/1r1o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r1o ConSurf].
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<div style="clear:both"></div>
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'''Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase'''
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==See Also==
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*[[Arginase 3D structures|Arginase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to form L-ornithine plus urea. Chiral L-amino acids bearing sulfonamide side chains have been synthesized in which the tetrahedral sulfonamide groups are designed to target bridging coordination interactions with the binuclear manganese cluster in the arginase active site. Syntheses of the amino acid sulfonamides have been accomplished by the amination of sulfonyl halide derivatives of (S)-(tert-butoxy)-[(tert-butoxycarbonyl)amino]oxoalkanoic acids. Amino acid sulfonamides with side chains comparable in length to that of L-arginine exhibit inhibition in the micromolar range, and the X-ray crystal structure of arginase I complexed with one of these inhibitors, S-(2-sulfonamidoethyl)-L-cysteine, has been determined at 2.8 A resolution. In the enzyme-inhibitor complex, the sulfonamide group displaces the metal-bridging hydroxide ion of the native enzyme and bridges the binuclear manganese cluster with an ionized NH(-) group. The binding mode of the sulfonamide inhibitor may mimic the binding of the tetrahedral intermediate and its flanking transition states in catalysis. It is notable that the ionized sulfonamide group is an excellent bridging ligand in this enzyme-inhibitor complex; accordingly, the sulfonamide functionality can be considered in the design of inhibitors targeting other binuclear metalloenzymes.
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[[Category: Large Structures]]
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==About this Structure==
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1R1O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1O OCA].
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==Reference==
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Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase., Cama E, Shin H, Christianson DW, J Am Chem Soc. 2003 Oct 29;125(43):13052-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14570477 14570477]
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[[Category: Arginase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Cama E]]
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[[Category: Cama, E.]]
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[[Category: Christianson DW]]
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[[Category: Christianson, D W.]]
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[[Category: Shin H]]
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[[Category: Shin, H.]]
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[[Category: Arginase]]
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[[Category: Hydrolase]]
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[[Category: Sulfonamide]]
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[[Category: Transition-state analogue]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:58:02 2008''
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Current revision

Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase

PDB ID 1r1o

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