2gvg: Difference between revisions

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

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

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~~'''~~Crystal Structure of human NMPRTase and its complex with NMN~~'''~~

===Crystal Structure of human NMPRTase and its complex with NMN===

~~==Overview==~~

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~~Nicotinamide phosphoribosyltransferase (NMPRTase) has a crucial role in the salvage pathway of NAD+ biosynthesis~~, ~~and a potent inhibitor of NMPRTase~~, ~~FK866, can reduce cellular NAD+ levels and induce apoptosis in tumors. We have determined~~ the ~~crystal structures~~ at ~~up to 2~~.~~1-A resolution of human and murine NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866~~. ~~The structures suggest that Asp219 is a determinant of substrate specificity of NMPRTase~~, ~~which~~ is ~~confirmed by our mutagenesis studies. FK866 is bound in a tunnel at the interface of~~ the NMPRTase dimer, and mutations in this binding site can abolish the inhibition by FK866. Contrary to current knowledge, the structures show that FK866 should compete directly with the nicotinamide substrate. Our structural and biochemical studies provide a starting point for the development of new anticancer agents.

The line below this paragraph, {{ABSTRACT_PUBMED_16783377}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16783377 is the PubMed ID number.

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==About this Structure==

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[[Category: Pbef]]

[[Category: Visfatin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 05~~:35:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:31:05 2008''

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-[[Image:2gvg.gif|left|200px]]
+{{Seed}}
+[[Image:2gvg.png|left|200px]]
 <!--
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 {{STRUCTURE_2gvg|  PDB=2gvg  |  SCENE=  }}
-'''Crystal Structure of human NMPRTase and its complex with NMN'''
+===Crystal Structure of human NMPRTase and its complex with NMN===
-==Overview==
+<!--
-Nicotinamide phosphoribosyltransferase (NMPRTase) has a crucial role in the salvage pathway of NAD+ biosynthesis, and a potent inhibitor of NMPRTase, FK866, can reduce cellular NAD+ levels and induce apoptosis in tumors. We have determined the crystal structures at up to 2.1-A resolution of human and murine NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. The structures suggest that Asp219 is a determinant of substrate specificity of NMPRTase, which is confirmed by our mutagenesis studies. FK866 is bound in a tunnel at the interface of the NMPRTase dimer, and mutations in this binding site can abolish the inhibition by FK866. Contrary to current knowledge, the structures show that FK866 should compete directly with the nicotinamide substrate. Our structural and biochemical studies provide a starting point for the development of new anticancer agents.
+The line below this paragraph, {{ABSTRACT_PUBMED_16783377}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16783377 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16783377}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Pbef]]
 [[Category: Visfatin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:35:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:31:05 2008''