1h69

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{Seed}}
 
[[Image:1h69.png|left|200px]]
[[Image:1h69.png|left|200px]]
Line 20: Line 19:
==About this Structure==
==About this Structure==
-
1H69 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H69 OCA].
+
[[1h69]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H69 OCA].
==Reference==
==Reference==
-
<ref group="xtra">PMID:11587640</ref><references group="xtra"/>
+
<ref group="xtra">PMID:11587640</ref><ref group="xtra">PMID:10706635</ref><ref group="xtra">PMID:10917652</ref><ref group="xtra">PMID:10433694</ref><ref group="xtra">PMID:7568029</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Amzel, L M.]]
[[Category: Amzel, L M.]]
Line 34: Line 33:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Rossman fold]]
[[Category: Rossman fold]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:45:07 2009''
 

Revision as of 22:10, 14 March 2011

Template:STRUCTURE 1h69

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,3,5,6,TETRAMETHYL-P-BENZOQUINONE (DUROQUINONE) AT 2.5 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 11587640

About this Structure

1h69 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM. Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones. Structure. 2001 Aug;9(8):659-67. PMID:11587640
  • Faig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM. Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3177-82. PMID:10706635 doi:http://dx.doi.org/10.1073/pnas.050585797
  • Bianchet MA, Foster C, Faig M, Talalay P, Amzel LM. Structure and mechanism of cytosolic quinone reductases. Biochem Soc Trans. 1999 Aug;27(4):610-5. PMID:10917652
  • Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM. Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry. 1999 Aug 3;38(31):9881-6. PMID:10433694 doi:http://dx.doi.org/10.1021/bi990799v
  • Li R, Bianchet MA, Talalay P, Amzel LM. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8846-50. PMID:7568029

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools