Sandbox Reserved 967: Difference between revisions
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==Structure of the Mouse RNase H2 Complex== | ==Structure of the Mouse RNase H2 Complex== | ||
<StructureSection load='3kio' size='1000' side='right' caption='mouse RNase H2 complex, (PDB code [[3kio]])> | <StructureSection load='3kio' size='1000' side='right' caption='mouse RNase H2 complex, (PDB code [[3kio]])> | ||
'''The RNase H2 ribonuclease complex''' is a heterotrimeric endoribonuclease responsible for the major ribonuclease H activity in mammalian cells. In mouse, the complex is encoded by 3 genes located on chromosomes 8 (''Rnaseh2a''), 14 (''Rnaseh2b'') and 19 (''Rnaseh2c'')<ref> http://genome-euro.ucsc.edu/cgi-bin/hgTracks?clade=mammal&org=Mouse&db=mm10&position=RnaseH2&hgt.positionInput=RnaseH2&hgt.suggestTrack=knownGene&Submit=submit&hgsid=201143152_yP1Xd4bMnHS7DV0d3VcqpDSxzzuQ&pix=1563</ref>. This enzyme specifically cleaves the 3’O-Phosphate bond of RNA in a DNA/RNA hybrids to produce 5’ phosphate and 3’hydroxyl ends. | '''The RNase H2 ribonuclease complex''' is a heterotrimeric endoribonuclease responsible for the major ribonuclease H activity in mammalian cells. In mouse, the complex is encoded by 3 genes located on chromosomes 8 (''Rnaseh2a''), 14 (''Rnaseh2b'') and 19 (''Rnaseh2c'')<ref> http://genome-euro.ucsc.edu/cgi-bin/hgTracks?clade=mammal&org=Mouse&db=mm10&position=RnaseH2&hgt.positionInput=RnaseH2&hgt.suggestTrack=knownGene&Submit=submit&hgsid=201143152_yP1Xd4bMnHS7DV0d3VcqpDSxzzuQ&pix=1563</ref>. This enzyme specifically cleaves the 3’O-Phosphate bond of RNA in a DNA/RNA hybrids to produce 5’ phosphate and 3’hydroxyl ends. | ||
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The complex is stabilized by the intimately interwoven architecture of H2B and H2C: The N-terminal region of H2B protein (amino acids 1-92) weaves together with H2C domain to form 3 β-barrels, also called “triple barrel”<ref name ="ref9"> Nicholson, Allen W. Ribonucleases. Springer Science & Business Media, 2011.</ref>. This triple barrel is formed from a total of 18 β-sheets and produces a pseudo-2-fold axis of symmetry along the central barrel. Also, it permits to leave the mostly α-helical C-terminal region of H2B available for potential interactions with other protein (for example the PCNA protein). Finally, it has been found that the motif provides a platform for securely binding the H2A protein: the side and end of the first barrel in the subcomplex H2B/H2C form a <scene name='60/604486/Tight_interface_h2ah2c/2'>tight interface</scene> with amino acids 197-258 in the C-terminal region of H2A protein. This interface is mainly composed of hydrophobic residues <ref name="ref5">. | The complex is stabilized by the intimately interwoven architecture of H2B and H2C: The N-terminal region of H2B protein (amino acids 1-92) weaves together with H2C domain to form 3 β-barrels, also called “triple barrel”<ref name ="ref9"> Nicholson, Allen W. Ribonucleases. Springer Science & Business Media, 2011.</ref>. This triple barrel is formed from a total of 18 β-sheets and produces a pseudo-2-fold axis of symmetry along the central barrel. Also, it permits to leave the mostly α-helical C-terminal region of H2B available for potential interactions with other protein (for example the PCNA protein). Finally, it has been found that the motif provides a platform for securely binding the H2A protein: the side and end of the first barrel in the subcomplex H2B/H2C form a <scene name='60/604486/Tight_interface_h2ah2c/2'>tight interface</scene> with amino acids 197-258 in the C-terminal region of H2A protein. This interface is mainly composed of hydrophobic residues <ref name="ref5">. | ||
== Interactions with nucleic acids == | |||
== == Interactions with nucleic acids == == | |||
It has been proved that the position of RNA/DNA complex in the active site cleft is determined by several favorable electrostatic interactions between the nucleic acid and positively charged amino acids of the protein<ref name = "ref2">. | It has been proved that the position of RNA/DNA complex in the active site cleft is determined by several favorable electrostatic interactions between the nucleic acid and positively charged amino acids of the protein<ref name = "ref2">. | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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Anaïs Bourbigot & Valériane Keïta | Anaïs Bourbigot & Valériane Keïta | ||
