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TitleMechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6.
Journal, issue, pagesSci Adv, Vol. 4, Issue 8, Page eaau6088, Year 2018
Publish dateAug 15, 2018
AuthorsAppu K Singh / Luke L McGoldrick / Edward C Twomey / Alexander I Sobolevsky /
PubMed AbstractCalcium (Ca) plays a major role in numerous physiological processes. Ca homeostasis is tightly controlled by ion channels, the aberrant regulation of which results in various diseases including ...Calcium (Ca) plays a major role in numerous physiological processes. Ca homeostasis is tightly controlled by ion channels, the aberrant regulation of which results in various diseases including cancers. Calmodulin (CaM)-mediated Ca-induced inactivation is an ion channel regulatory mechanism that protects cells against the toxic effects of Ca overload. We used cryo-electron microscopy to capture the epithelial calcium channel TRPV6 (transient receptor potential vanilloid subfamily member 6) inactivated by CaM. The TRPV6-CaM complex exhibits 1:1 stoichiometry; one TRPV6 tetramer binds both CaM lobes, which adopt a distinct head-to-tail arrangement. The CaM carboxyl-terminal lobe plugs the channel through a unique cation-π interaction by inserting the side chain of lysine K115 into a tetra-tryptophan cage at the pore's intracellular entrance. We propose a mechanism of CaM-mediated Ca-induced inactivation that can be explored for therapeutic design.
External linksSci Adv / PubMed:30116787 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 3.9 Å
Structure data

8961

6e2f

EMDB-8961, PDB-6e2f:
Cryo-EM structure of human TRPV6 in complex with Calmodulin
Method: EM (single particle) / Resolution: 3.9 Å

8962

6e2g

EMDB-8962, PDB-6e2g:
Cryo-EM structure of rat TRPV6 in complex with Calmodulin
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / TRPV6 / TRP channels / Calcium channels

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