1gcu: Difference between revisions

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[[Image:1gcu.jpg|left|200px]]
{{Seed}}
[[Image:1gcu.png|left|200px]]


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{{STRUCTURE_1gcu|  PDB=1gcu  |  SCENE=  }}  
{{STRUCTURE_1gcu|  PDB=1gcu  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A'''
===CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A===




==Overview==
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Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.
The line below this paragraph, {{ABSTRACT_PUBMED_11224565}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11224565}}


==About this Structure==
==About this Structure==
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[[Category: Biliverdin]]
[[Category: Biliverdin]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
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