Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin.

Schumacher MA, Rivard AF, Baechinger HP, Adelman JP

Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening ... [more]

Nature Apr. 26, 2001; 410(6832);1120-4 [Pubmed: 11323678]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

KCNN2

Gene Ontology Biological Process

Gene Ontology Molecular Function

alpha-actinin binding [IPI]calcium-activated potassium channel activity [IDA]calmodulin binding [IBA]protein homodimerization activity [IPI]small conductance calcium-activated potassium channel activity [IBA, TAS]

Gene Ontology Cellular Component