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 R301A 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 R301A in IRK11_MOUSE

Point mutation:	R301A
Domain:	C-term
General numbering (KChannelDB):	-
Protein:	IRK11_MOUSE (Kcnj1)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 301 in IRK11_MOUSE
Other point mutations / same protein	List of mutations in IRK11_MOUSE
Family alignments	Inward rectifiers (Kir) Potassium channels 2 TMs
Other point mutations / same position	Position 294 in Inward rectifiers (Kir) family Position 294 in Potassium channels 2 TMs family
Reference:	Stabilization of the activity of ATP-sensitive potassium channels by ion pairs formed between adjacent Kir6.2 subunits. Lin YW, Jia T, Weinsoft AM, Shyng SL J Gen Physiol 2003 Aug;122(2):225-37.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

R301A

Three of the arginine-to-alanine mutations (R192A , R301A , and R314A) that exhibited reduced response to exogenously applied PIP2 also displayed rapid spontaneous decay of currents after membrane excision into ATP-free solutions , a behavior which we have termed 'inactivation' (Shyng et al. , 2000b(image) )
Specifically , we tested whether the R192A , R301A , and R314A mutations cause channel inactivation by disrupting electrostatic interactions within the channel complex
Through systematic mutation of each of the negatively charged residues in the cytoplasmic regions of Kir6.2 to alanine , we found that mutation E229A also induces fast channel inactivation similar to that seen in the R192A , R301A , and R314A mutants
RESULTS (image)TOP (image)ABSTRACT (image)INTRODUCTION (image)MATERIALS AND METHODS (image)RESULTS (image)DISCUSSION (image)REFERENCES Mutation of Glutamate 229 in Kir6.2 to Alanine Induces K ATP Channel Inactivation K ATP currents generated by coexpression of SUR1 and Kir6.2 mutants R192A , R301A , or R314A have been shown previously to inactivate after inside-out patch excision into ATP-free solutions (Shyng et al. , 2000b(image) )
1 B , and 2 , A and B) , with characteristics similar to those seen with the R192A , R301A , and R314A channels (Shyng et al. , 2000b(image) )
Under the same recording condition , the inactivation time constants were 4.79 ą 1.34 , 0.32 ą 0.03 , and 3.08 ą 0.43 s for R192A , R301A , and R314A channels , respectively (n = 7-9 patches in each case as shown in Table I ; the slow current decay in WT could not be fit by a single exponential , therefore no value was given)
Aside from exposure to ATP and subsequent removal of ATP , PIP2 can also reverse channel inactivation caused by the E229A mutation , similar to that found in the R192A , R301A , or R314A mutant channels (Shyng et al. , 2000b(image) )

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