2bzg
CRYSTAL STRUCTURE OF THIOPURINE S-METHYLTRANSFERASE.
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OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
2BZG is a [Single protein] structure of sequence from [Homo sapiens] with SAH and B3P as [ligands]. Active as [Thiopurine S-methyltransferase], with EC number [2.1.1.67]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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