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 L262I 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 L262I in IRK3_HUMAN

Point mutation:	L262I
Domain:	C-term
General numbering (KChannelDB):	-
Protein:	IRK3_HUMAN (KCNJ3,GIRK)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in IRK3_HUMAN
Family alignments	Inward rectifiers (Kir) Potassium channels 2 TMs
Other point mutations / same position	Position 243 in Inward rectifiers (Kir) family Position 243 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.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

L262I

Fig. 5 A shows that G1*(L262I) , the mutant corresponding to G4*(L268I) , greatly reduced but did not abolish basal G1* 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
The G1(L262I) caused even less inhibition of heteromeric G1(L262I) / G4 currents , consistent with its effects in G1* homomers (Fig. 5 A)
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)
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))

F.Horn (kchanneldbcmbi.ru.nl), 17-Aug-2005