Sandbox Reserved 967: Difference between revisions
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It has been shown that the Mammalian RNase complex is a heteromeric complex formed by 3 distinct proteins: <scene name='60/604486/H2a/1'>H2A</scene>,<scene name='60/604486/H2b/1'>H2B</scene> and <scene name='60/604486/H2c/1'>H2C</scene>. H2A protein is the catalytic subunit and H2B/H2C proteins are auxiliary subunits: they are structural domains that facilitate cohesion of the complex<ref name="ref5"> Shaban, Nadine M., Scott Harvey, Fred W. Perrino, and Thomas Hollis. “The Structure of the Mammalian RNase H2 Complex Provides Insight into RNA•DNA Hybrid Processing to Prevent Immune Dysfunction.” Journal of Biological Chemistry 285, no. 6 (February 5, 2010): 3617–24. [http://dx.doi.org/10.1074/jbc.M109.059048 doi:10.1074/jbc.M109.059048.]</ref>. | It has been shown that the Mammalian RNase complex is a heteromeric complex formed by 3 distinct proteins: <scene name='60/604486/H2a/1'>H2A</scene>,<scene name='60/604486/H2b/1'>H2B</scene> and <scene name='60/604486/H2c/1'>H2C</scene>. H2A protein is the catalytic subunit and H2B/H2C proteins are auxiliary subunits: they are structural domains that facilitate cohesion of the complex<ref name="ref5"> Shaban, Nadine M., Scott Harvey, Fred W. Perrino, and Thomas Hollis. “The Structure of the Mammalian RNase H2 Complex Provides Insight into RNA•DNA Hybrid Processing to Prevent Immune Dysfunction.” Journal of Biological Chemistry 285, no. 6 (February 5, 2010): 3617–24. [http://dx.doi.org/10.1074/jbc.M109.059048 doi:10.1074/jbc.M109.059048.]</ref>. | ||
The first domain structure of the complex, H2A, contains 301 amino acids, almost as H2B protein which computes 308 amino acids. H2C protein is the smallest subunit: it only has 166 amino acids. | The first domain structure of the complex, H2A, contains 301 amino acids, almost as H2B protein which computes 308 amino acids. H2C protein is the smallest subunit: it only has 166 amino acids. | ||
Each of these proteins adopts various secondary structures with β-strands and α-helices: | Each of these proteins adopts various <scene name="/12/3456/Sample/2"> secondary structures </scene> with β-strands and α-helices: | ||
*H2A protein has 12 α-helices, 11 β-strands and 3 turns<ref> http://www.uniprot.org/uniprot/Q9CWY8</ref>, | *H2A protein has 12 α-helices, 11 β-strands and 3 turns<ref> http://www.uniprot.org/uniprot/Q9CWY8</ref>, | ||
*H2B molecule computes 8 α-helices, 7 β-strands and 3 turns<ref> http://www.uniprot.org/uniprot/Q80ZV0</ref>, | *H2B molecule computes 8 α-helices, 7 β-strands and 3 turns<ref> http://www.uniprot.org/uniprot/Q80ZV0</ref>, | ||
