EF-hand containing protein

EF-hand containing proteins are a large and structurally diverse superfamily defined by the presence of the EF-hand motif, a helix–loop–helix structural domain that binds calcium ions with high selectivity, mediating processes ranging from calcium signaling to buffering[1][2][3][5][6]. Members include calmodulin, troponin C, parvalbumin, S100 family, and many others, with functions spanning from regulatory (signal transduction via conformational change upon Ca2+ binding) to structural (buffering intracellular calcium without major conformational change)[2][5][6]. This is not a single protein or "target" in the sense used for drug discovery, but rather a defining motif within many functionally specialized proteins; thus, listing the family alone ("EF-hand containing proteins") is too broad to match specific therapeutic targeting or indication[1][5]. As a family, there are no broadly interacting compounds; some individual members such as calmodulin have interacting compounds (e.g., trifluoperazine), but the entire group is not broadly targetable. "EF-hand containing proteins" is an imprecise entry if used as a druggable target; it refers to a protein superfamily, not an individual molecular entity. For drug discovery or biomarker use, a specific protein such as "Calmodulin" or "S100B" should be used[1][5][6].

Other names

EF-hand proteinEF-hand calcium-binding protein

Calcium binding induces conformational changes, modulating interaction with various target proteins[2][6]