2bzg

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{{Seed}}
 
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[[Image:2bzg.png|left|200px]]
 
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==Crystal structure of thiopurine S-methyltransferase.==
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The line below this paragraph, containing "STRUCTURE_2bzg", creates the "Structure Box" on the page.
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<StructureSection load='2bzg' size='340' side='right'caption='[[2bzg]], [[Resolution|resolution]] 1.58&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'>[[2bzg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZG 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]] 1.58&#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=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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{{STRUCTURE_2bzg| PDB=2bzg | 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=2bzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzg OCA], [https://pdbe.org/2bzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzg RCSB], [https://www.ebi.ac.uk/pdbsum/2bzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzg ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN] Defects in TPMT are the cause of thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:[https://omim.org/entry/610460 610460]. TPMT is an enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosupressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus.
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== Function ==
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[https://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN] Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.<ref>PMID:18484748</ref>
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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/bz/2bzg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2bzg 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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Human thiopurine S-methyltransferase (TPMT) exhibits considerable person-to-person variation in activity to thiopurine drugs. We have produced an N-terminal truncation of human TPMT protein, crystallized the protein in complex with the methyl donor product S-adenosyl-L-homocysteine, and determined the atomic structure to the resolution of 1.58 and 1.89 A, respectively, for the seleno-methionine incorporated and wild type proteins. The structure of TPMT indicates that the naturally occurring amino acid polymorphisms scatter throughout the structure, and that the amino acids whose alteration have the most influence on function are those that form intra-molecular stabilizing interactions (mainly van der Waals contacts). Furthermore, we have produced four TPMT mutant proteins containing variant alleles of TPMT*2, *3A, *3B, and *3C and examined the structure-function relationship of the mutant proteins based on their expression and solubility in bacteria and their thermostability profile.
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===CRYSTAL STRUCTURE OF THIOPURINE S-METHYLTRANSFERASE.===
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Structural basis of allele variation of human thiopurine-S-methyltransferase.,Wu H, Horton JR, Battaile K, Allali-Hassani A, Martin F, Zeng H, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Cheng X Proteins. 2007 Apr 1;67(1):198-208. PMID:17243178<ref>PMID:17243178</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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The line below this paragraph, {{ABSTRACT_PUBMED_17243178}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2bzg" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17243178 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17243178}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2BZG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZG OCA].
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==Reference==
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<ref group="xtra">PMID:17243178</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Thiopurine S-methyltransferase]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Battaile, K P.]]
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[[Category: Battaile KP]]
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[[Category: Bochkarev, A.]]
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[[Category: Bochkarev A]]
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[[Category: Dong, A.]]
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[[Category: Dong A]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Loppnau, P.]]
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[[Category: Loppnau P]]
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[[Category: Plotnikov, A N.]]
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[[Category: Plotnikov AN]]
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[[Category: Sgc, Structural Genomics Consortium.]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M.]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J.]]
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[[Category: Wu H]]
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[[Category: Wu, H.]]
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[[Category: Zeng H]]
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[[Category: Zeng, H.]]
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[[Category: Methyltransferase]]
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[[Category: Polymorphism]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:48:59 2009''
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Current revision

Crystal structure of thiopurine S-methyltransferase.

PDB ID 2bzg

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