Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres

摘要

The structure of hSurvivin bound to the histone H3 tail phosphorylated on Thr-3 was solved to determine how the CPC reads the histone code. Many eukaryotes have two Survivin paralogues. A major difference between them is that class A is pH sensitive in H3T3ph binding, whereas class B is relatively pH insensitive but has lower affinity for H3T3ph.