2z7g: Difference between revisions

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{{Seed}}
[[Image:2z7g.png|left|200px]]


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==Crystal structure of adenosine deaminase ligated with EHNA==
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<StructureSection load='2z7g' size='340' side='right'caption='[[2z7g]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2z7g]] 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=2Z7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z7G FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52&#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=EH9:(2S,3R)-3-(6-AMINO-9H-PURIN-9-YL)NONAN-2-OL'>EH9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2z7g|  PDB=2z7g  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z7g OCA], [https://pdbe.org/2z7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z7g RCSB], [https://www.ebi.ac.uk/pdbsum/2z7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z7g ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z7/2z7g_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2z7g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adenosine deaminase (ADA) perpetuates chronic inflammation by degrading extracellular adenosine which is toxic for lymphocytes. ADA has two distinct conformations: open form and closed form. From the crystal structures with various ligands, the non-nucleoside type inhibitors bind to the active site occupying the critical water-binding-position and sustain the open form of apo-ADA. In contrast, substrate mimics do not occupy the critical position, and induce the large conformational change to the closed form. However, it is difficult to predict the binding of (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), as it possesses characteristic parts of both the substrate and the non-nucleoside inhibitors. The crystal structure shows that EHNA binds to the open form through a novel recognition of the adenine base accompanying conformational change from the closed form of the PR-ADA complex in crystalline state.


===Crystal structure of adenosine deaminase ligated with EHNA===
Conformational change of adenosine deaminase during ligand-exchange in a crystal.,Kinoshita T, Tada T, Nakanishi I Biochem Biophys Res Commun. 2008 Aug 15;373(1):53-7. Epub 2008 Jun 10. PMID:18549808<ref>PMID:18549808</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2z7g" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18549808}}, adds the Publication Abstract to the page
*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18549808 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18549808}}
__TOC__
 
</StructureSection>
==About this Structure==
2Z7G 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=2Z7G OCA].
 
==Reference==
Conformational change of adenosine deaminase during ligand-exchange in a crystal., Kinoshita T, Tada T, Nakanishi I, Biochem Biophys Res Commun. 2008 Aug 15;373(1):53-7. Epub 2008 Jun 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18549808 18549808]
[[Category: Adenosine deaminase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kinoshita, T.]]
[[Category: Kinoshita T]]
[[Category: Acetylation]]
[[Category: Beta barrel]]
[[Category: Hydrolase]]
[[Category: Nucleotide metabolism]]
[[Category: Pharmaceutical]]
[[Category: Polymorphism]]
[[Category: Protein-inhibitor complex]]
 
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Retrieved from "https://proteopedia.org/2z7g"