2bzg: Difference between revisions

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==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.

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==

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[[Category: Single protein]]

[[Category: Thiopurine S-methyltransferase]]

[[Category: Arrowsmith, C.H.]]

[[Category: Arrowsmith, C H.]]

[[Category: Battaile, K.P.]]

[[Category: Battaile, K P.]]

[[Category: Bochkarev, A.]]

[[Category: Dong, A.]]

[[Category: Edwards, A.M.]]

[[Category: Edwards, A M.]]

[[Category: Loppnau, P.]]

[[Category: Plotnikov, A.N.]]

[[Category: Plotnikov, A N.]]

[[Category: Sgc, Structural.Genomics.Consortium.]]

[[Category: Sgc, Structural Genomics Consortium.]]

[[Category: Sundstrom, M.]]

[[Category: Weigelt, J.]]

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[[Category: transferase]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 17: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Thiopurine S-methyltransferase]]
-[[Category: Arrowsmith, C.H.]]
+[[Category: Arrowsmith, C H.]]
-[[Category: Battaile, K.P.]]
+[[Category: Battaile, K P.]]
 [[Category: Bochkarev, A.]]
 [[Category: Dong, A.]]
-[[Category: Edwards, A.M.]]
+[[Category: Edwards, A M.]]
 [[Category: Loppnau, P.]]
-[[Category: Plotnikov, A.N.]]
+[[Category: Plotnikov, A N.]]
-[[Category: Sgc, Structural.Genomics.Consortium.]]
+[[Category: Sgc, Structural Genomics Consortium.]]
 [[Category: Sundstrom, M.]]
 [[Category: Weigelt, J.]]
@@ Line 38: / Line 38: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:29:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:16 2008''