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Document Page 203 not form stable dimers was sequenced [48]. This ADH mutant has alanine-159 replaced with threonine. A 3D model of Drosophila ADH shows alanine-159 on the opposite surface of α helix F from tyrosine- 153 and lysine-157 [48]. Alanine-159 along with alanine-158 form a hydrophobic anchor that stabilizes the dimer interface. These two residues of ADH and the homologous residues in other short-chain alcohol dehydrogenases have been overlooked in sequence analyses because they are not absolutely conserved. In fact, at least five amino acids are found in these positions among the different sec-alcohol dehydrogenases. G. Dimer Interface in 11β-and 17β-Hydroxysteroid Dehydrogenases Because α helix F at the dimer interface also contains the catalytic tyrosine and the nearby lysine residue, any structural analysis of the catalytic site must also consider the structure of this part of the dimer interface. For this reason, we modeled α helix F on 11β-HSD-1 and -2 and 17β-HSD-1, -2, -3, and -4 to gain an insight into stabilizing interactions and how they may affect the catalytic site. H. Human 11β-HSD-1 Figure 5 shows the modeled structure for the α helix F interface in human 11β-HSD-1, in which phenylalanine-188 and alanine-189 form an anchor. Alanine-189 is 3.5 Å and 4.7 Å from alanine-189 and alanine-185, respectively, on the other subunit. The phenylalanine-188 side chain is 3.2 Å from glycine-192. There is a hydrogen bond between serine-185 and serine-196, which are 3.2 Å apart. Alanine-185 is 4.7 Å from phenylalanine-193. There also is a hydrophobic interaction between phenylalanine-193 and alanine-181, which are 3.9 Å apart. This web of interaction between side chains on the outer surface of α helix F on each subunit influences residues that have side chains oriented to the interior where catalysis occurs. Alanine-185, which is stabilized by interactions with phenylalanine-193, and serine-184, which interacts with serine-196, are between the conserved tyrosine-183 and lysine-187. Phenylalanine-193 is adjacent to phenylalanine- 194, which is positioned into the catalytic site. I. Human 11β-HSD-2 Figure 5 shows the α helix F interface of human 11β-HSD-2. Alanine-237 is about 3 Å from leucine- 241; alanine-238 is about 3.7 Å from both alanine-238 and threonine-234. Threonine-234 has a stabilizing hydrophobic interaction http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_203.html [4/5/2004 5:06:03 PM]
Document Figure 6 Structure of α helix F interface of mammalian 17β-hydroxysteroid dehydrogenases. The α helix F part of the dimer interface on 17β-hydroxysteroid dehydrogenases is shown along with side chains of the highly conserved tyrosine and lysine residues and three other residues that are oriented into the cavity that binds substrate and nucleotide cofactor. (a) Modeled structure of human 17β-hydroxysteroid dehydrogenase type 1. (b) Modeled structure of human 17β-hydroxysteroid dehydrogenase type 2. (c) Modeled structure of human 17β-hydroxysteroid dehydrogenase type 3. (d) Modeled structure of porcine 17β-hydroxysteroid dehydrogenase type 4. with leucine-242, which is 4.2 Å distant. Threonine-245 is 4.2 Å from the C α carbon of glycine-230. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_204.html (1 of 2) [4/5/2004 5:06:14 PM] Page 204
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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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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document [Protease targets] serinyl
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