1vfl

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{{Seed}}
 
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[[Image:1vfl.png|left|200px]]
 
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==Adenosine deaminase==
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The line below this paragraph, containing "STRUCTURE_1vfl", creates the "Structure Box" on the page.
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<StructureSection load='1vfl' size='340' side='right'caption='[[1vfl]], [[Resolution|resolution]] 1.80&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'>[[1vfl]] 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=1VFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VFL 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]] 1.8&#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=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1vfl| PDB=1vfl | 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=1vfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfl OCA], [https://pdbe.org/1vfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vfl RCSB], [https://www.ebi.ac.uk/pdbsum/1vfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vfl 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/vf/1vfl_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=1vfl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Adenosine deaminase===
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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:16060665<ref>PMID:16060665</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1vfl" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16060665}}, adds the Publication Abstract to the page
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*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16060665 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16060665}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1VFL is a 1 chain 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=1VFL OCA].
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==Reference==
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<ref group="xtra">PMID:16060665</ref><references group="xtra"/>
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[[Category: Adenosine deaminase]]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Kinoshita, T.]]
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[[Category: Large Structures]]
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[[Category: Beta-barel]]
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[[Category: Kinoshita T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:07:14 2009''
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Current revision

Adenosine deaminase

PDB ID 1vfl

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