1gcu

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{{STRUCTURE_1gcu| PDB=1gcu | SCENE= }}
{{STRUCTURE_1gcu| PDB=1gcu | SCENE= }}
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'''CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A'''
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===CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11224565 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:06:13 2008''

Revision as of 02:06, 1 July 2008

Image:1gcu.png

Template:STRUCTURE 1gcu

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Template:ABSTRACT PUBMED 11224565

About this Structure

1GCU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of rat biliverdin reductase., Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y, Nat Struct Biol. 2001 Mar;8(3):221-5. PMID:11224565

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