Sandbox Reserved 1741: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
HIV reverse transcriptase is an asymmetric heterodimer. There are 560 residues in Chain A, shown in blue, and 440 residues in Chain B, shown in green (3). The RNase H domain is absent in Chain B, p51, resulting in a different folding pattern from Chain A, p66. In both chains, Alpha helices and Beta sheets can be found. Globular proteins represent the tertiary structure since both secondary structures are present. | HIV reverse transcriptase is an asymmetric heterodimer. There are 560 residues in Chain A, shown in blue, and 440 residues in Chain B, shown in green (3). The RNase H domain is absent in Chain B, p51, resulting in a different folding pattern from Chain A, p66. In both chains, Alpha helices and Beta sheets can be found. Globular proteins represent the tertiary structure since both secondary structures are present. The structure to the right shows an ATB molecule attached to the p66 subunit. | ||
== References == | == References == | ||
<references/> | <references/> | ||
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(8) Sluis-Cremer, N.; Tachedjian, G. Mechanisms of Inhibition of HIV Replication by Non- | (8) Sluis-Cremer, N.; Tachedjian, G. Mechanisms of Inhibition of HIV Replication by Non- | ||
Nucleoside Reverse Transcriptase Inhibitors. ''Virus Res.'' '''2008''', ''134'' (1-2), 147–156. | Nucleoside Reverse Transcriptase Inhibitors. ''Virus Res.'' '''2008''', ''134'' (1-2), 147–156. | ||
