2pqt
From Proteopedia
(New page: 200px<br /> <applet load="2pqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pqt, resolution 1.780Å" /> '''Human N-acetyltran...) |
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| - | [[Image:2pqt.gif|left|200px]]<br /> | + | [[Image:2pqt.gif|left|200px]]<br /><applet load="2pqt" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2pqt" size=" | + | |
caption="2pqt, resolution 1.780Å" /> | caption="2pqt, resolution 1.780Å" /> | ||
'''Human N-acetyltransferase 1'''<br /> | '''Human N-acetyltransferase 1'''<br /> | ||
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==Overview== | ==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. | 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. | ||
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| - | ==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== | ||
| - | 2PQT 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 CL and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arylamine_N-acetyltransferase Arylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.5 2.3.1.5] Full crystallographic information is available from [http:// | + | 2PQT 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=CL:'>CL</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arylamine_N-acetyltransferase Arylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.5 2.3.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:41:16 2008'' |
Revision as of 10:41, 23 January 2008
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Human N-acetyltransferase 1
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.
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 Wed Jan 23 12:41:16 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
