2h11: Difference between revisions
m Protected "2h11" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_2h11| PDB=2h11 | SCENE= }} | {{STRUCTURE_2h11| PDB=2h11 | SCENE= }} | ||
===Amino-terminal Truncated Thiopurine S-Methyltransferase Complexed with S-Adenosyl-L-Homocysteine=== | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN]] Defects in TPMT are the cause of thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:[http://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. | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/TPMT_HUMAN TPMT_HUMAN]] Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.<ref>PMID:18484748</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[2h11]] is a 2 chain structure with 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=2H11 OCA]. | [[2h11]] is a 2 chain structure with 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=2H11 OCA]. | ||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Thiopurine S-methyltransferase]] | [[Category: Thiopurine S-methyltransferase]] | ||
Revision as of 07:44, 25 March 2013
Amino-terminal Truncated Thiopurine S-Methyltransferase Complexed with S-Adenosyl-L-HomocysteineAmino-terminal Truncated Thiopurine S-Methyltransferase Complexed with S-Adenosyl-L-Homocysteine
DiseaseDisease
[TPMT_HUMAN] Defects in TPMT are the cause of thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM: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.
FunctionFunction
[TPMT_HUMAN] Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.[1]
About this StructureAbout this Structure
2h11 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Peng Y, Feng Q, Wilk D, Adjei AA, Salavaggione OE, Weinshilboum RM, Yee VC. Structural basis of substrate recognition in thiopurine s-methyltransferase. Biochemistry. 2008 Jun 10;47(23):6216-25. Epub 2008 May 17. PMID:18484748 doi:10.1021/bi800102x