BACKGROUND: Loss-of-function mutations in the voltage gated @entity972 channel Kv 11.1 have been associated with the @entity1162 ( @entity1162 ) type 2. We identified the @entity70186 mutation in Kv 11.1 in a family with @entity1162 . @entity70187 is located in the outer part of the pore helix, a structure that is involved in C-type inactivation. Here we characterize the effect of @entity70186 on the functional properties of KV 11.1. METHODS: The @entity70186 mutation was introduced into KV 11.1 ( @entity70187 ). @entity196 ( @entity7097 ) and @entity70187 were expressed in @entity1238 oocytes and characterized by two-electrode-voltage-clamp. RESULTS: @entity70187 currents were reduced to <20% of @entity7097 currents and @entity70187 induced a minor negative shift in half maximal rectification, indicating that the voltage-dependent onset on inactivation occurred at more negative voltages compared to @entity7097 . Co-expression of @entity70187 with @entity7097 revealed intermediate phenotype and there was no dominant negative effect of @entity70187 . CONCLUSION: These findings suggest that @entity70186 causes a loss-of-function of Kv 11.1. This results in a reduced repolarizing reserve which may result in LQTS2 and @entity1164 .

The Mutation P.T613a in the Pore Helix of the Kv 11.1 @entity972 Channel is Associated with XXXX .

@entity1164 :: ('MESH:D016757', 'Disease') :: ['sudden cardiac death'] @entity70187 :: ('c|SUB|T|613|A', 'DNAMutation') :: ['T613A'] @entity1238 :: ('8355', 'Species') :: ['Xenopus laevis'] @entity7097 :: ('MESH:C536751', 'Disease') :: ['WT'] @entity196 :: ('MESH:D020754', 'Disease') :: ['Wild-type KV 11.1'] @entity972 :: ('MESH:D011188', 'Chemical') :: ['potassium'] @entity1162 :: ('MESH:D008133', 'Disease') :: ['LQTS', 'Long QT Syndrome'] @entity70186 :: ('p|SUB|T|613|A', 'ProteinMutation') :: ['p.T613A']
@entity1162 :: (MESH:D008133,Disease) :: ['Long QT Syndrome']
