A helix-breaking mutation in the epithelial Ca(2+) channel TRPV5 leads to reduced Ca(2+)-dependent inactivation.
Lee
Kyu Pil
KP
Department of Physiology, Radboud University Nijmegen Medical Centre, The Netherlands.
Nair
Anil V
AV
Grimm
Christian
C
van Zeeland
Femke
F
Heller
Stefan
S
Bindels
René J M
RJ
Hoenderop
Joost G J
JG
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000502:physiology; D002118:Calcium / Q000037:antagonists & inhibitors / Q000378:metabolism*; D015220:Calcium Channels / Q000235:genetics; D057809:HEK293 Cells; D018257:Helix-Loop-Helix Motifs; D006801:Humans; D007668:Kidney / Q000502:physiology; D051379:Mice; D008969:Molecular Sequence Data; D053499:Plasma Membrane Calcium-Transporting ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism; D017354:Point Mutation; D011392:Proline / Q000037:antagonists & inhibitors / Q000378:metabolism; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D050916:TRPV Cation Channels / Q000037:antagonists & inhibitors* / Q000235:genetics* / Q000378:metabolism; D050051:Transient Receptor Potential Channels
D015220:Calcium Channels; C510642:MCOLN3 protein, human; D050916:TRPV Cation Channels; C492239:TRPV5 protein, human; C422827:TRPV6 protein, human; D050051:Transient Receptor Potential Channels; C492240:Trpv5 protein, mouse; C446923:Trpv6 protein, mouse; D011392:Proline; D053499:Plasma Membrane Calcium-Transporting ATPases; D002118:Calcium