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Document http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_198.html (1 of 2) [4/5/2004 5:05:32 PM] Page 198
Document Figure 4 Amino acids important in cofactor and catalysis in human 11b-hydroxysteroid dehydrogenase types 1 and 2. (a) 11b-HSD type 1. Preference of 11b-HSD type 1 for NADPH resides in lysine-44 and arginine-66, which have positively charged side chains that stabilize the binding of the 2'-phosphate on NADPH. These residues also counteract the repulsive interaction between glutamic acid 69 and the phosphate group. (b) 11b-HSD type 2. Preference of 11b-HSD type 2 for NAD+ is due to favorable bonds with aspartic acid-91, serine-92, and threonine-112. Moreover there is a coulombic repulsion between aspartic acid-91 and NADP+, which destabilizes binding of NADP+ 11b-HSD type 2 lacks a near<strong>by</strong> amino acid with a positively charged side chain that could diminish the repulsive interaction between NADP+ and aspartic acid-91. Also shown are threonine residues that could hydrogen bond to nicotinamide's carboxamidemoiety. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_198.html (2 of 2) [4/5/2004 5:05:32 PM]
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Structure-based Drug Design 14 Stru
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Document 106. Cirino NM, Cameron CE
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Document 122. Marshall WS, Beaton G
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Document We determined the structur
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Page 195 and 196: Document large solvent channels and
Page 197 and 198: Document IV. Drug Design Progressio
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Page 201 and 202: Document Table 1 Inhibition Data fo
Page 203 and 204: Document Page 166 As predicated, th
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 215 and 216: Document Page 176 0.43 Å) as the c
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Page 221 and 222: Document Page 182 (SAR) model. The
Page 223 and 224: Document IX. S2' Interactions Page
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Document A. The Canyon Page 491 The
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Document Page 495 of the RNA and pr
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Document Figure 4 A ribbon diagram
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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