2pqt: Difference between revisions

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[[Image:2pqt.~~gif~~|left|200px]]

[[Image:2pqt.png|left|200px]]

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~~'''~~Human N-acetyltransferase 1~~'''~~

===Human N-acetyltransferase 1===

~~==Overview==~~

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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 line below this paragraph, {{ABSTRACT_PUBMED_17656365}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17656365 is the PubMed ID number.

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==About this Structure==

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[[Category: Sgc]]

[[Category: Structural genomics consortium]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 13~~:38:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:46:13 2008''

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-[[Image:2pqt.gif|left|200px]]
+{{Seed}}
+[[Image:2pqt.png|left|200px]]
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 {{STRUCTURE_2pqt|  PDB=2pqt  |  SCENE=  }}
-'''Human N-acetyltransferase 1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17656365}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17656365 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17656365}}
 ==About this Structure==
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 [[Category: Sgc]]
 [[Category: Structural genomics consortium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:38:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:46:13 2008''