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Oxidoreductase PDB id
1ads
Jmol
Contents
Protein chain
315 a.a. *
Ligands
NAP
Waters ×104
* Residue conservation analysis
PDB id:
1ads
Name: Oxidoreductase
Title: An unlikely sugar substrate site in the 1.65 angstroms structure of the human aldose reductase holoenzyme implicated in diabetic complications
Structure: Aldose reductase. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.65Å     R-factor:   0.200    
Authors: D.K.Wilson,F.A.Quiocho
Key ref: D.K.Wilson et al. (1992). An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science, 257, 81-84. PubMed id: 1621098 DOI: 10.1126/science.1621098
Date:
08-Jul-92     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P15121  (ALDR_HUMAN) -  Aldose reductase
Seq:
Struc: 		316 a.a.
315 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.1.1.21  - Aldehyde reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Alditol + NAD(P)(+) = aldose + NAD(P)H
Alditol
 +
NAD(P)(+)
Bound ligand (Het Group name = NAP)
corresponds exactly 		= aldose
 + NAD(P)H
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   3 terms 
  Biological process     response to stress   4 terms 
  Biochemical function     electron carrier activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1126/science.1621098 Science 257:81-84 (1992)
PubMed id: 1621098  
 
 
An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.
D.K.Wilson, K.M.Bohren, K.H.Gabbay, F.A.Quiocho.
 
  ABSTRACT  
 
Aldose reductase, which catalyzes the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reduction of a wide variety of aromatic and aliphatic carbonyl compounds, is implicated in the development of diabetic and galactosemic complications involving the lens, retina, nerves, and kidney. A 1.65 angstrom refined structure of a recombinant human placenta aldose reductase reveals that the enzyme contains a parallel beta 8/alpha 8-barrel motif and establishes a new motif for NADP-binding oxidoreductases. The substrate-binding site is located in a large, deep elliptical pocket at the COOH-terminal end of the beta barrel with a bound NADPH in an extended conformation. The highly hydrophobic nature of the active site pocket greatly favors aromatic and apolar substrates over highly polar monosaccharides. The structure should allow for the rational design of specific inhibitors that might provide molecular understanding of the catalytic mechanism, as well as possible therapeutic agents.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
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PDB codes: 2bgq 2bgs 2vdg
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PDB codes: 3bur 3buv 3bv7 3cmf 3cot
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PDB codes: 2qxw 2r24
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Functional genomic studies of aldo-keto reductases.
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Isolation of a non-covalent aldose reductase-nucleotide-inhibitor complex.
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Aldose and aldehyde reductases: correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active site.
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  Curr Opin Struct Biol, 10, 456-461.  
10651037 Q.Ye, D.Hyndman, X.Li, T.G.Flynn, and Z.Jia (2000).
Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily.
  Proteins, 38, 41-48.
PDB code: 1c9w
10737928 S.Khurana, G.Sanli, D.B.Powers, S.Anderson, and M.Blaber (2000).
Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases.
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10399921 J.M.Gulbis, S.Mann, and R.MacKinnon (1999).
Structure of a voltage-dependent K+ channel beta subunit.
  Cell, 97, 943-952.
PDB code: 1qrq
10387026 K.Ratnam, H.Ma, and T.M.Penning (1999).
The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3 alpha-hydroxysteroid dehydrogenase, a representative aldo-keto reductase.
  Biochemistry, 38, 7856-7864.  
9918192 L.Costantino, G.Rastelli, P.Vianello, G.Cignarella, and D.Barlocco (1999).
Diabetes complications and their potential prevention: aldose reductase inhibition and other approaches.
  Med Res Rev, 19, 3.  
10339620 M.B.Burg, E.M.Peters, K.M.Bohren, and K.H.Gabbay (1999).
Factors affecting counteraction by methylamines of urea effects on aldose reductase.
  Proc Natl Acad Sci U S A, 96, 6517-6522.  
  10493576 M.Young, K.Kirshenbaum, K.A.Dill, and S.Highsmith (1999).
Predicting conformational switches in proteins.
  Protein Sci, 8, 1752-1764.  
10584067 P.Várnai, W.G.Richards, and P.D.Lyne (1999).
Modelling the catalytic reaction in human aldose reductase.
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Structural and kinetic determinants of aldehyde reduction by aldose reductase.
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10089480 V.Lamour, P.Barth, H.Rogniaux, A.Poterszman, E.Howard, A.Mitschler, A.Van Dorsselaer, A.Podjarny, and D.Moras (1999).
Production of crystals of human aldose reductase with very high resolution diffraction.
  Acta Crystallogr D Biol Crystallogr, 55, 721-723.  
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Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a "push-pull" mechanism for proton transfer in aldo-keto reductases.
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Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine.
  Biochemistry, 37, 11003-11011.  
9730277 H.Lee (1998).
The structure and function of yeast xylose (aldose) reductases.
  Yeast, 14, 977-984.  
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Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: stereochemical and kinetic evidence.
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9657682 J.M.Jez, and T.M.Penning (1998).
Engineering steroid 5 beta-reductase activity into rat liver 3 alpha-hydroxysteroid dehydrogenase.
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Aldose reductase: a window to the treatment of diabetic complications?
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Mutational analysis of the role of the conserved lysine-270 in the Pichia stipitis xylose reductase.
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Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution.
  Proc Natl Acad Sci U S A, 95, 6768-6773.
PDB code: 1a80
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Kinetic studies of FR-1, a growth factor-inducible aldo-keto reductase.
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9454604 W.Neuhauser, D.Haltrich, K.D.Kulbe, and B.Nidetzky (1998).
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Catalytic mechanism of aldose reductase studied by the combined potentials of quantum mechanics and molecular mechanics.
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A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.
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PDB codes: 1ah0 1ah3 1ah4
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PDB code: 1afs
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PDB code: 1ae4
9095201 Z.J.Liu, Y.J.Sun, J.Rose, Y.J.Chung, C.D.Hsiao, W.R.Chang, I.Kuo, J.Perozich, R.Lindahl, J.Hempel, and B.C.Wang (1997).
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PDB code: 1ad3
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Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family.
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PDB code: 1cyd
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PDB code: 1ofg
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Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens.
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Hydration in drug design. 1. Multiple hydrogen-bonding features of water molecules in mediating protein-ligand interactions.
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Residues affecting the catalysis and inhibition of rat lens aldose reductase.
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All in the family.
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Structure of porcine aldehyde reductase holoenzyme.
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7542775 S.W.Chouinard, G.F.Wilson, A.K.Schlimgen, and B.Ganetzky (1995).
A potassium channel beta subunit related to the aldo-keto reductase superfamily is encoded by the Drosophila hyperkinetic locus.
  Proc Natl Acad Sci U S A, 92, 6763-6767.  
  7641075 T.Terada (1995).
Role of lysine residues in the nucleotides binding to bovine liver high-Km aldehyde reductase.
  Int J Biochem Cell Biol, 27, 457-467.  
8048162 D.Bossemeyer (1994).
The glycine-rich sequence of protein kinases: a multifunctional element.
  Trends Biochem Sci, 19, 201-205.  
7508385 K.H.Kondo, M.H.Kai, Y.Setoguchi, G.Eggertsen, P.Sjöblom, T.Setoguchi, K.I.Okuda, and I.Björkhem (1994).
Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme.
  Eur J Biochem, 219, 357-363.  
  7881908 K.M.Fox, and P.A.Karplus (1994).
Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.
  Structure, 2, 1089-1105.
PDB codes: 1oya 1oyb 1oyc
8146147 S.S.Hoog, J.E.Pawlowski, P.M.Alzari, T.M.Penning, and M.Lewis (1994).
Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily.
  Proc Natl Acad Sci U S A, 91, 2517-2521.
PDB code: 1ral
  8110701 T.A.Gardiner, A.W.Stitt, H.R.Anderson, and D.B.Archer (1994).
Selective loss of vascular smooth muscle cells in the retinal microcirculation of diabetic dogs.
  Br J Ophthalmol, 78, 54-60.  
8001150 T.McCormack, and K.McCormack (1994).
Shaker K+ channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily.
  Cell, 79, 1133-1135.  
8234324 D.K.Wilson, I.Tarle, J.M.Petrash, and F.A.Quiocho (1993).
Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.
  Proc Natl Acad Sci U S A, 90, 9847-9851.
PDB code: 1mar
8234296 E.M.Ellis, D.J.Judah, G.E.Neal, and J.D.Hayes (1993).
An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases.
  Proc Natl Acad Sci U S A, 90, 10350-10354.  
8497486 I.Dubchak, S.R.Holbrook, and S.H.Kim (1993).
Prediction of protein folding class from amino acid composition.
  Proteins, 16, 79-91.  
8444164 J.Jeffery, B.Persson, I.Wood, T.Bergman, R.Jeffery, and H.Jörnvall (1993).
Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure.
  Eur J Biochem, 212, 41-49.  
8281941 M.Jaquinod, N.Potier, K.Klarskov, J.M.Reymann, O.Sorokine, S.Kieffer, P.Barth, V.Andriantomanga, J.F.Biellmann, and A.Van Dorsselaer (1993).
Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.
  Eur J Biochem, 218, 893-903.  
8141995 S.Janecek, and S.Baláz (1993).
Evolution of parallel beta/alpha-barrel enzyme family lightened by structural data on starch-processing enzymes.
  J Protein Chem, 12, 509-514.  
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