KChannelDB: Extraction of mutation data from the literature 2005, KChannelDB.
This data was extracted from Medline abstracts and full texts (when available) in an automated manner.
The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation H57F was found are listed after the table.
The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.
Point mutation H57F in IRK3_HUMAN
|General numbering (KChannelDB):|| -|
|Other point mutations / same protein||List of mutations in IRK3_HUMAN|
Inward rectifiers (Kir)|
Potassium channels 2 TMs
|Other point mutations / same position||
Position 36 in Inward rectifiers (Kir) family |
Position 36 in Potassium channels 2 TMs family
|Reference:||Identification of critical residues controlling G protein-gated inwardly rectifying K(+) channel activity through interactions with the beta gamma subunits of G proteins.|
He C, Yan X, Zhang H, Mirshahi T, Jin T, Huang A, Logothetis DE
J Biol Chem 2002 Feb 22;277(8):6088-96.
|Other point mutations / same article||List|
|Text source||HTML full text|
|Validation status||Not yet checked|
- In contrast , the N-terminal GIRK1* mutant G1*(H57F) behaved as the corresponding G4*(H64F) , abolishing completely K + currents
- As expected , the double mutant G1*(H57F , L262I) , containing the non-functional H57F mutation , abolished all G1* currents
- Fig. 5 B shows that the G1 / G4(H64F , L268I) heteromeric channels showed no activity , in contrast to the G1(H57F , L262I) / G4 channels that exhibited small inwardly rectifying K + currents
- When both mutant subunits were coexpressed , G1(H57F , L262I) and G4(H64F , L268I) , no K + currents could be measured
- Of the G1 mutants , the G1(H57F) / G4 heteromers also showed greatly attenuated K + currents , whereas the G1(L262I) / G4 showed attenuated but larger heteromeric currents than any of the other mutant / wild-type combinations
- Each of the G1 mutant combinations with G4 wild-type , G1(H57F) / G4 , G1(L262I) / G4 , and G1(H57F , L262I) / G4 , showed clear peaks in their amplitude histograms , indicating that functional heteromeric channels were formed
- G1(H57F) also greatly reduced but did not abolish heteromeric G1(H57F) / G4 currents
- A , representative traces of cell attached recordings from Xenopus oocytes expressing GIRK4 / GIRK1(G4 / G1) , G4 alone , G4 / G1(H57F) , G4 / G1(L262I) , G4 / G1(H57F , L262I)
- Mutations of G beta gamma -interacting residues that abolished basal currents also showed no agonist-induced currents (e.g. GIRK4*(H64F) , GIRK4*(L268I) , or GIRK1*(H57F))
- On the other hand , mutations that attenuated but did not abolish basal currents also preserved agonist-induced responses (e.g. GIRK1*(L262I) or heteromeric channels of wild-type GIRK4 with mutant GIRK1(H57F) , GIRK1(L262I) , or GIRK1(H57F , L262I))
- The N-terminal GIRK channel mutations (GIRK4-H64F and GIRK1-H57F) abolished all K + currents
F.Horn (kchanneldbcmbi.ru.nl), 17-Aug-2005