2bzg

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[[Image:2bzg.gif|left|200px]]<br /><applet load="2bzg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bzg.gif|left|200px]]
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caption="2bzg, resolution 1.58&Aring;" />
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'''CRYSTAL STRUCTURE OF THIOPURINE S-METHYLTRANSFERASE.'''<br />
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{{Structure
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|PDB= 2bzg |SIZE=350|CAPTION= <scene name='initialview01'>2bzg</scene>, resolution 1.58&Aring;
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|SITE= <scene name='pdbsite=AC1:B3p+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> and <scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Thiopurine_S-methyltransferase Thiopurine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.67 2.1.1.67]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THIOPURINE S-METHYLTRANSFERASE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BZG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=B3P:'>B3P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thiopurine_S-methyltransferase Thiopurine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.67 2.1.1.67] Known structural/functional Site: <scene name='pdbsite=AC1:B3p+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZG OCA].
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2BZG is a [[Single protein]] 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].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17243178 17243178]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17243178 17243178]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:48 2008''

Revision as of 14:08, 20 March 2008

Image:2bzg.gif


PDB ID 2bzg

Drag the structure with the mouse to rotate
, resolution 1.58Å
Sites:
Ligands: and
Activity: Thiopurine S-methyltransferase, with EC number 2.1.1.67
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THIOPURINE S-METHYLTRANSFERASE.


Contents

Overview

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.

Disease

Known disease associated with this structure: 6-mercaptopurine sensitivity OMIM:[187680]

About this Structure

2BZG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Mar 20 16:08:48 2008

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