Sandbox Reserved 958: Difference between revisions
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This protein is divided in three main domains: the N-terminal, the central and the C-terminal domain. | This protein is divided in three main domains: the N-terminal, the central and the C-terminal domain. | ||
The '''N-terminal domain''' presents a HHCC motif which is a pseudo zinc-finger complexing with zinc ions. The zinc ejection impedes the 3'-processing process and pertubs the integrase multimerisation<ref name="Carayon">PMID:20164093</ref>. Therefore the presence of this ion is necessary the virus life cycle. | The '''N-terminal domain''' (1-49) presents a HHCC motif which is a pseudo zinc-finger complexing with zinc ions. The zinc ejection impedes the 3'-processing process and pertubs the integrase multimerisation<ref name="Carayon">PMID:20164093</ref>. Therefore the presence of this ion is necessary the virus life cycle. | ||
The '''central domain''' which corresponds to the catalytic domain contains the <scene name='60/604477/Catalytic_triad/1'>catalytic triad</scene> by association of two aspartates and one glutamate residues that coordinate bivalent ions, Cd++ in this structure but Mg++ or Mn++ ''in vivo'' <ref name="Liao">PMID:21426159</ref>. There is also an analogy of structure with the transposase core domain. This domain contains <scene name='60/604477/Structure/2'>residues</scene> between the 170-180 position involved in the packaging of the Uracil DNA glycosylase ('''UNG2''')<ref name="Zheng">PMID:23863879</ref> essential for the viral replication. | The '''central domain''' (50-213) which corresponds to the catalytic domain contains the <scene name='60/604477/Catalytic_triad/1'>catalytic triad</scene> by association of two aspartates and one glutamate residues that coordinate bivalent ions, Cd++ in this structure but Mg++ or Mn++ ''in vivo'' <ref name="Liao">PMID:21426159</ref>. There is also an analogy of structure with the transposase core domain. This domain contains <scene name='60/604477/Structure/2'>residues</scene> between the 170-180 position involved in the packaging of the Uracil DNA glycosylase ('''UNG2''')<ref name="Zheng">PMID:23863879</ref> essential for the viral replication. | ||
The '''C-terminale domain''' allows the DNA binding in a non-specific manner and | The '''flexible elbow''' (195-220) is a 26-aa alpha-helix called alpha 6 helix links the C-ter domain to the catalytic core domain. It can be see like a flexible elbow because it offers conformation changes of the two previous domains during integration. Another property of this intermediary domain is the ability to contact the DNA phosphate backbone thanks to three main residues : K211, K215 and K219. | ||
The '''C-terminale domain''' (214-288) is a domain composed of five beta-sheets. It allows the DNA binding in a non-specific manner, HIV-1 IN dimer-dimer contacts, has a tethering role for DNA during the integration process and is also involved in the stability of the complex with DNA<ref name="Tsuruyama">PMID:23341952</ref>. | |||
== DNA binding == | == DNA binding == | ||