2gwu

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:2gwu.png|left|200px]]
 
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==STRUCTURE MODEL OF HUMAN ARYLAMINE N-ACETYLTRANSFERASE 1==
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The line below this paragraph, containing "STRUCTURE_2gwu", creates the "Structure Box" on the page.
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<StructureSection load='2gwu' size='340' side='right'caption='[[2gwu]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gwu FirstGlance], [https://www.ebi.ac.uk/pdbsum/2gwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwu ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2gwu| PDB=2gwu | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Arylamine N-acetyltransferases (NATs) catalyze the acetylation of arylamines, a key step in the detoxification of many carcinogens. The determinants of NAT substrate specificity are not known, yet this knowledge is required to understand why NAT enzymes acetylate some arylamines, but not others. Here, we use NMR spectroscopy and homology modeling to reveal the structural determinants of arylamine acetylation by NATs. In particular, by using chemical shift perturbation analysis, we have identified residues that play a critical role in substrate binding and catalysis. This study reveals why human NAT1 acetylates the sunscreen additive p-aminobenzoic acid and tobacco smoke carcinogen 4-aminobiphenyl, but not o-toluidine and other arylamines linked to bladder cancer. Our results represent an important step toward predicting whether arylamines present in new products can be detoxified by mammalian NATs.
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===STRUCTURE MODEL OF HUMAN ARYLAMINE N-ACETYLTRANSFERASE 1===
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NMR-based model reveals the structural determinants of mammalian arylamine N-acetyltransferase substrate specificity.,Zhang N, Liu L, Liu F, Wagner CR, Hanna PE, Walters KJ J Mol Biol. 2006 Oct 13;363(1):188-200. Epub 2006 Aug 15. PMID:16959263<ref>PMID:16959263</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16959263}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2gwu" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16959263 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16959263}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWU OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:16959263</ref><references group="xtra"/>
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[[Category: Hanna, P E]]
[[Category: Hanna, P E]]
[[Category: Liu, F]]
[[Category: Liu, F]]
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[[Category: Walters, K J]]
[[Category: Walters, K J]]
[[Category: Zhang, N]]
[[Category: Zhang, N]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:07:15 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

STRUCTURE MODEL OF HUMAN ARYLAMINE N-ACETYLTRANSFERASE 1

PDB ID 2gwu

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