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Document Table 1 Percent Identity Between Hydroxysteroid Dehydrogenase Sequences Shown in Figure 3 Page 197 11β-HSD-2 17β-HSD-2 17β-HSD-3 17β-HSD-1 11β-HSD-1 17β-HSD-4 11β-HSD-2 0.00 46.1 20.3 28.6 20.6 18.1 17β-HSD-2 0.0 21.1 21.2 17.7 18.9 17β-HSD-3 0.0 19.1 19.6 17.5 17β-HSD-1 0.0 21.1 20.4 11β-HSD-1 0.0 17.1 17β-HSD-4 0.0 dehydrogenases. Knowledge of structure-activity relationships for the binding site on steroid dehydrogenases will be helpful in identifying novel compounds from plants and other sources that could be useful in regulating steroid dehydrogenases. At this time, we are just beginning to work on this ambitious goal. Structural information is limited. The 3-D structure of 17β-HSD type 1 has been determined [28], but without the steroid or cofactor in the binding site. Fortunately, 11β-HSD and 17β-HSD belong to a large family of enzymes that are called short-chain alcohol dehydrogenases [29–31] or sec-alcohol dehydrogenases [32]. The structures of dehydrogenase homologs in bacteria, plants, and animals have been determined [33–37] and we used them as templates for modeling 11β-HSD and 17β-HSD [38,39]. There also is information about the effects of mutations on catalytic activity in 11β-HSD-1 [40] and 17β-HSD-1 [41] and in homologs, especially for Drosophila alcohol dehydrogenase (ADH) [42–48]. Together they enable us to begin to understand the relationship between structure and function in hydroxysteroid dehydrogenases, as we discuss in this chapter. II. Methods A. Molecular Modeling http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_197.html (1 of 2) [4/5/2004 5:05:25 PM]
Document Important for the validity of the models that we constructed is the evidence from models of other proteins indicating that two proteins can have as little as 20 to 25% sequence identity and still have very similar 3D structures, especially in α helices and β stands [49–52]. Variation is found in the loops and coiled structures. A relevant example for this chapter is the comparison of the tertiary structure of rat dihydropteridine reductase [33] and Streptomyces hydrogenans 20β-hydroxysteroid dehydrogenase [34]. As noted <strong>by</strong> Varughese et al. [33], despite less than 20% sequence identity between dihydropteridine reductase and http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_197.html (2 of 2) [4/5/2004 5:05:25 PM]
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Structure-based Drug Design 14 Stru
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Document dine) and didanosine (dide
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Document 4 Bradykinin Receptor Anta
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Page 205 and 206: Document References 1. Parks RE Jr.
Page 207 and 208: Document 17. Ealick SE, Rule SA, Ca
Page 209 and 210: Document 6 Structural Implications
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Page 233 and 234: Document 7 Structure—Function Rel
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Page 257 and 258: Document 29. Baker ME. Genealogy of
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Document Table 1 Approval Indicatio
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Document Page 438 proteins. One pot
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Document Subsequent studies have sh
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Document Figure 5 Some compounds wh
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Document Cyclotheonamide A (CtA), 2
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document fragment-based programs, 5
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Document [Human immunodeficiency vi
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Document Kininogen, 119 high molecu
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Document Phosphoglycerate kinase (P
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Document [Protease targets] serinyl
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