2pqt
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The human arylamine N-acetyltransferases NAT1 and NAT2 play an important | + | The human arylamine N-acetyltransferases NAT1 and NAT2 play an important role in the biotransformation of a plethora of aromatic amine and hydrazine drugs. They are also able to participate in the bioactivation of several known carcinogens. Each of these enzymes is genetically variable in human populations, and polymorphisms in NAT genes have been associated with various cancers. Here we have solved the high resolution crystal structures of human NAT1 and NAT2, including NAT1 in complex with the irreversible inhibitor 2-bromoacetanilide, a NAT1 active site mutant, and NAT2 in complex with CoA, and have refined them to 1.7-, 1.8-, and 1.9-A resolution, respectively. The crystal structures reveal novel structural features unique to human NATs and provide insights into the structural basis of the substrate specificity and genetic polymorphism of these enzymes. |
| + | |||
| + | ==Disease== | ||
| + | Known disease associated with this structure: Orthostatic intolerance OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163970 163970]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 13: | ||
==Reference== | ==Reference== | ||
| - | Structural | + | Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases., Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN, J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17656365 17656365] |
[[Category: Arylamine N-acetyltransferase]] | [[Category: Arylamine N-acetyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
[[Category: Bochkarev, A.]] | [[Category: Bochkarev, A.]] | ||
[[Category: Dombrovski, L.]] | [[Category: Dombrovski, L.]] | ||
| - | [[Category: Edwards, A | + | [[Category: Edwards, A M.]] |
| - | [[Category: Grant, D | + | [[Category: Grant, D M.]] |
[[Category: Loppnau, P.]] | [[Category: Loppnau, P.]] | ||
| - | [[Category: Plotnikov, A | + | [[Category: Plotnikov, A N.]] |
| - | [[Category: SGC, Structural | + | [[Category: SGC, Structural Genomics Consortium.]] |
[[Category: Sundstrom, M.]] | [[Category: Sundstrom, M.]] | ||
[[Category: Tempel, W.]] | [[Category: Tempel, W.]] | ||
| Line 36: | Line 39: | ||
[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:06 2008'' |
Revision as of 16:32, 21 February 2008
|
Human N-acetyltransferase 1
Contents |
Overview
The human arylamine N-acetyltransferases NAT1 and NAT2 play an important role in the biotransformation of a plethora of aromatic amine and hydrazine drugs. They are also able to participate in the bioactivation of several known carcinogens. Each of these enzymes is genetically variable in human populations, and polymorphisms in NAT genes have been associated with various cancers. Here we have solved the high resolution crystal structures of human NAT1 and NAT2, including NAT1 in complex with the irreversible inhibitor 2-bromoacetanilide, a NAT1 active site mutant, and NAT2 in complex with CoA, and have refined them to 1.7-, 1.8-, and 1.9-A resolution, respectively. The crystal structures reveal novel structural features unique to human NATs and provide insights into the structural basis of the substrate specificity and genetic polymorphism of these enzymes.
Disease
Known disease associated with this structure: Orthostatic intolerance OMIM:[163970]
About this Structure
2PQT is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Arylamine N-acetyltransferase, with EC number 2.3.1.5 Full crystallographic information is available from OCA.
Reference
Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases., Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN, J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. PMID:17656365
Page seeded by OCA on Thu Feb 21 18:32:06 2008
Categories: Arylamine N-acetyltransferase | Homo sapiens | Single protein | Arrowsmith, C H. | Bochkarev, A. | Dombrovski, L. | Edwards, A M. | Grant, D M. | Loppnau, P. | Plotnikov, A N. | SGC, Structural Genomics Consortium. | Sundstrom, M. | Tempel, W. | Weigelt, J. | Wu, H. | CL | UNX | Arylamide acetylase 1 | Arylamine n-acetyltransferase 1 | Bromoacetanilide | Covalent | Inhibitor | Sgc | Structural genomics consortium
