Structure of the SPRY domain of human Ash2L and its interactions with RbBP5 and DPY30.

The article discusses the crystal structure of SPRY domain of human Absent, small or homeotic discs-like 2 (Ash2L), and its interactions with nuclear protein DPY30 and retinoblastoma-binding protein 5 (RbBP5). It notes the role of SPRY domain as a primary moiety in Ash2L that recognizes RbBP5, mediates MLL1 complex assembly, and regulates MLL1 enzymatic activity. It also cites the correlation of structural disparities in its loop regions with their role in specific protein recognition.