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Document Figure 6 Superposition of the NNRTIs in the HIV-1 RT/TIBO complex [35], HIV-1 RT/α-APA complex [34], and HIV-1 RT/nevirapine complex [32]. The side chains are shown for those amino acid residues that have close contacts with bound inhibitors and the three catalytically essential aspartic acids in the HIV-1 RT/TIBO complex. Most of the amino acid residues that form the NNIBP are hydrophobic. Though the NNRTIs are chemically and structurally diverse, the bound NNRTIs all assume a strikingly common butterfly-like shape. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_57.html [4/5/2004 4:50:13 PM] Page 57
Document Table 3 HIV-1 RT Amino Acid Residues Defining the Nonnucleoside Inhibitor-Binding Pocket (NNIBP) and the Locations of NNRTI-Resistance Mutations (see also [12]) NNIBP Residues Pro95 β5 Location Mutation Possible Effects References Ala98 β5–β6 Gly less bulky 9,164 Leu100 β5–β6 Ile β-branch 9,164-166 Lys101 β5–β6 Glu charge change 164 Lys103 β5–β6 Asn, Gln charge loss, less bulky 9,24,164 Val106 β6 Ala less bulky 9,58,165 Val108 β6 Ile bulkier 9,164 Glu138 β7–β8(p51) Lys charge change 166 Val179 β9 Glu, Asp charge gain, bulkier 164 Tyr181 β9 Cys, Ile aromaticity loss, less bulky 24,58,164 Tyr188 β10 His, Cys, Leu aromaticity loss, less bulky 9,167 Gly190 β10 Glu charge gain, bulkier 9,22,168 Phe227 β12 Leu228 β12 Phe aromaticity gain, bulkier 133 Trp229 β12 Glu233 β13 Val charge loss, less bulky 169 Leu234 β13 Pro236 β13–β14 Leu increase flexibility, bulkier 133 Lys238 β14 Thr charge loss, less bulky 133 Tyr318 β15 http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_58.html (1 of 2) [4/5/2004 4:50:15 PM] Page 58
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Structure-based Drug Design 14 Stru
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Page 103 and 104: Document dine) and didanosine (dide
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Document D ddI, 152 tumour necrosis
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Document [Protease targets] serinyl
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