1hdo: Difference between revisions

Revision as of 08:02, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hdo.png

Template:STRUCTURE 1hdo

HUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEXHUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEX

Template:ABSTRACT PUBMED 11224564

About this StructureAbout this Structure

1HDO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme., Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M, Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564

Page seeded by OCA on Tue Jul 1 08:02:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''HUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEX'''
+===HUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEX===
-==Overview==
+<!--
-Biliverdin IXbeta reductase (BVR-B) catalyzes the pyridine nucleotide-dependent production of bilirubin-IXbeta, the major heme catabolite during early fetal development. BVR-B displays a preference for biliverdin isomers without propionates straddling the C10 position, in contrast to biliverdin IXalpha reductase (BVR-A), the major form of BVR in adult human liver. In addition to its tetrapyrrole clearance role in the fetus, BVR-B has flavin and ferric reductase activities in the adult. We have solved the structure of human BVR-B in complex with NADP+ at 1.15 A resolution. Human BVR-B is a monomer displaying an alpha/beta dinucleotide binding fold. The structures of ternary complexes with mesobiliverdin IValpha, biliverdin IXalpha, FMN and lumichrome show that human BVR-B has a single substrate binding site, to which substrates and inhibitors bind primarily through hydrophobic interactions, explaining its broad specificity. The reducible atom of both biliverdin and flavin substrates lies above the reactive C4 of the cofactor, an appropriate position for direct hydride transfer. BVR-B discriminates against the biliverdin IXalpha isomer through steric hindrance at the bilatriene side chain binding pockets. The structure also explains the enzyme's preference for NADP(H) and its B-face stereospecificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11224564}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11224564 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11224564}}
 ==About this Structure==
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 [[Category: Haem degradation]]
 [[Category: Methaemoglobin reductase]]
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