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Calmodulin binding domain

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Protein domain Protein family
CaMBD
solution structure of the calmodulin binding domain (cambd) of small conductanceCa-activated potassium channels (sk2)
Identifiers
SymbolCaMBD
PfamPF02888
InterProIPR004178
SCOP21kkd / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, calmodulin binding domain (CaMBD) is a protein domain found in small-conductance calcium-activated potassium channels (SK channels). These channels are independent of voltage and gated solely by intracellular Ca. They are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaMBD, which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca binds the EF hands in the N-lobe of CaM. The structure of this domain complexed with CaM is known. This domain forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other.

References

  1. ^ Schumacher MA, Rivard AF, Bachinger HP, Adelman JP (April 2001). "Structure of the gating domain of a Ca-activated K+ channel complexed with Ca/calmodulin". Nature. 410 (6832): 1120–4. Bibcode:2001Natur.410.1120S. doi:10.1038/35074145. PMID 11323678. S2CID 205016620.
This article incorporates text from the public domain Pfam and InterPro: IPR004178 Category: