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Document Page 199 20β-hydroxysteroid dehydrogenase, the root mean square deviation for the two tertiary structures is 2 Å over 160 C α carbon atoms. We aligned human 11β-HSD-1 [21] and 11β-HSD-2 [22] with S. hydrogenans 20β-hydroxysteroid dehydrogenase and Escherichia coli 7α-hydroxysteroid dehydrogenase [37] for 3D modeling. Human 11β-HSD has extra segments at the amino terminus and carboxyl terminus. Previously reported alignments [30,31,53] were used to find the core structure consisting of about 225 residues that are structurally similar to the template. The first 190 residues of the 255 residues are reasonably well conserved among the hydroxysteroid dehydrogenases. Alignment of the C-terminal 65 residues is less certain as this part contains gaps and insertions. Fortunately, the core 190 residues contains the catalytic site and the cofactor binding site. We also superimposed the two 11β-HSD structures on mouse carbonyl reductase [37]. The 11β-HSD 3D structures superimpose nicely on α helices E and F and other helices and strands that are important in binding of cofactor and substrate. Then, we extracted NADPH from carbonyl reductase and NAD + from 7α-hydroxysteroid dehydrogenase and inserted the cofactors into the structures of the two 11β-HSDs. The α helix F in 17β-HSD-1 [16], 17β-HSD-2 [17], 17β-HSD-3 [18], and porcine 17β-HSD-4 [26] was constructed by modeling on α helix F in 20β-hydroxysteroid dehydrogenase. Comparisons with other 3D structures [33–37] have demonstrated that this α helix is highly conserved. The modeled dimers were not minimized as a dimer complex to avoid the artifactual adjustment of α helix F side chains. The Homology program (Biosym Technologies, Inc., 1995) was used to model a 255-residue segment of 11β-HSD and α helix F of 17β-HSD on the S. hydrogenans 20β-hydroxysteroid dehydrogenase template. To produce the final model (Figures 4 and 5) this program finds an optimal configuration of the residues when arranged in the template structure by minimizing unfavorable interactions between amino acid side chains. The side chains of each monomer were then minimized (1,000 iterations of the conjugate gradient) using the Discover program (Biosym Technologies Inc., 1995). http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_199.html [4/5/2004 5:05:34 PM]
Document III. Results and Discussion Figure 5 Structure of α helix F interface of human 11β-hydroxysteroid dehydrogenase types 1 and 2. The α helix F part of the dimer interface on 11β-HSD-1 and -2 is shown along with side chains of the highly conserved tyrosine and lysine residues and other residues that are oriented into the cavity that binds substrate and nucleotide cofactor. A. NADPH Binding Site on 11β-Hydroxysteroid Dehydrogenase Types 1 and 2 Page 200 Several lines of evidence—sequence analysis, mutagenesis studies, and the solved 3D structure of homologs of 11β-HSD—indicate that the nucleotide binding site in these enzymes has many similarities to that in other classes of dehydrogenases. For many dehydrogenases, the nucleotide binding domain http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_200.html (1 of 2) [4/5/2004 5:05:58 PM]
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