1wxy

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[[Image:1wxy.gif|left|200px]]
 
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{{Structure
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==Crystal structure of adenosine deaminase ligated with a potent inhibitor==
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|PDB= 1wxy |SIZE=350|CAPTION= <scene name='initialview01'>1wxy</scene>, resolution 2.50&Aring;
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<StructureSection load='1wxy' size='340' side='right'caption='[[1wxy]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=FRK:N-[4,5-BIS(4-HYDROXYPHENYL)-1,3-THIAZOL-2-YL]HEXANAMIDE'>FRK</scene>
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<table><tr><td colspan='2'>[[1wxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WXY FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Adenosine_deaminase Adenosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4]
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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]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRK:N-[4,5-BIS(4-HYDROXYPHENYL)-1,3-THIAZOL-2-YL]HEXANAMIDE'>FRK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=1wxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wxy OCA], [https://pdbe.org/1wxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wxy RCSB], [https://www.ebi.ac.uk/pdbsum/1wxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wxy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADA_BOVIN ADA_BOVIN] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
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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/wx/1wxy_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=1wxy ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of adenosine deaminase ligated with a potent inhibitor'''
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==See Also==
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*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Structural snapshots corresponding to various states enable elucidation of the molecular recognition mechanism of enzymes. Adenosine deaminase has two distinct conformations, an open form and a closed form, although it has so far been unclear what factors influence adaptation of the alternative conformations. Herein, we have determined the first nonligated structure as an initial state, which was the open form, and have thereby rationally deduced the molecular recognition mechanism. Inspection of the active site in the nonligated and ligated states indicated that occupancy at one of the water-binding positions in the nonligated state was highly significant in determining alternate conformations. When this position is empty, subsequent movement of Phe65 toward the space induces the closed form. On the other hand, while occupied, the overall conformation remains in the open form. This structural understanding should greatly assist structure-oriented drug design and enable control of the enzymatic activity.
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==About this Structure==
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1WXY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WXY OCA].
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==Reference==
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Structural basis of compound recognition by adenosine deaminase., Kinoshita T, Nakanishi I, Terasaka T, Kuno M, Seki N, Warizaya M, Matsumura H, Inoue T, Takano K, Adachi H, Mori Y, Fujii T, Biochemistry. 2005 Aug 9;44(31):10562-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16060665 16060665]
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[[Category: Adenosine deaminase]]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kinoshita, T.]]
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[[Category: Kinoshita T]]
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[[Category: FRK]]
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[[Category: ZN]]
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[[Category: beta barel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:02:53 2008''
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Current revision

Crystal structure of adenosine deaminase ligated with a potent inhibitor

PDB ID 1wxy

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