Sandbox Reserved 958: Difference between revisions

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OCA, Charlene Hartnagel

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 In order to have a tight binding, the integrase-DNA interaction requires optimal number of contacts such as hydrogen bonds, van der Waals forces and ionic interactions between DNA elements (bases, phosphates and sugars) and amino acid chains. Among the alpha4 helix residues, <scene name='60/604477/Lys_residues_alpha4_helix/2'>Lys156 and Lys159</scene> have a main role in the specific binding of integrase to DNA by forming bidentate hydrogen bonds which are higher specific than single hydrogen bonds<ref name="Hobaika">PMID:19808934</ref>. Moreover, by being positively charged, the lysine side chain provides ionic interactions as well. In addition, Lys-rich sequence implicated in this specific interaction include these two lysines.
 It has also be shown that <scene name='60/604477/Gln_alpha4_helix/2'>Gln148 residue</scene> contacts on adenine and cytosine of the 5' AC overhang in processed LTR<ref name="Hobaika">PMID:19808934</ref>.
-It also seems that there is a different sensitivity to the viral DNA sequence (LTR) depending on the presence of Mg++ or Mn++ suggesting that specific contacts between the integrase and the viral DNA extremity are more favored in a Mg++ containing environment<ref name="Carayon">PMID:20164093</ref>.
+It also seems that there is a different sensitivity to the viral DNA sequences (LTRs) depending on the presence of Mg++ or Mn++ suggesting that specific contacts between the integrase and the viral DNA extremities are more favored in a Mg++ containing environment<ref name="Carayon">PMID:20164093</ref>.
 == Function ==