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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''' (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 for 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 for the virus life cycle.     


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 and <scene name='60/604477/Residues_186-194/1'>residues 186-194</scene> help to interact with DNA by contact the major groove of viral and cellular DNA<ref name="Chen">PMID:10890912</ref>. 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 Asp and one Glu''' 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 and <scene name='60/604477/Residues_186-194/1'>residues 186-194</scene> help to interact with DNA by contact the major groove of viral and cellular DNA<ref name="Chen">PMID:10890912</ref>. 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 '''flexible elbow''' (195-220) is a 26-aa alpha-helix called <scene name='60/604477/Flexible_elbow/1'>alpha 6</scene> helix that 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<ref name="Chen">PMID:10890912</ref>.
The '''flexible elbow''' (195-220) is a 26-aa alpha-helix called <scene name='60/604477/Flexible_elbow/1'>alpha 6</scene> helix that 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<ref name="Chen">PMID:10890912</ref>.

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OCA, Charlene Hartnagel