Sandbox Reserved 967: Difference between revisions
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=== Several interactions between the subunits === | === Several interactions between the subunits === | ||
H2C protein is found in the middle of the elongated complex structure, flanked by H2A and H2B proteins on the ends. | |||
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”. 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 tight interface with amino acids 197-258 in the C-terminal region of H2A protein. This interface is composed mainly of hydrophobic residues. | |||
== Interaction with nucleic acids == | == Interaction with nucleic acids == | ||
