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 R176V 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 R176V in KAT1_ARATH

Point mutation:	R176V
Cited point mutation:	Arg176Val,Arg176
Domain:	TRANSMEM IV
General numbering (KChannelDB):	455
Protein:	KAT1_ARATH (KAT1,At5g46240,MPL12.)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 176 in KAT1_ARATH
Other point mutations / same protein	List of mutations in KAT1_ARATH
Family alignments	AKT-like Inward rectifiers 6TMs Plant potassium channels
Other point mutations / same position	Position 178 in AKT-like Inward rectifiers 6TMs family Position 178 in Plant potassium channels family
Reference:	Molecular dissection of the contribution of negatively and positively charged residues in S2, S3, and S4 to the final membrane topology of the voltage sensor in the K+ channel, KAT1. Sato Y, Sakaguchi M, Goshima S, Nakamura T, Uozumi N J Biol Chem 2003 Apr 11;278(15):13227-34. Epub 2003 Jan 29.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

Arg176

To produce PL fusion proteins , DNA encoding Met1-Arg165 , Met1-Arg171 , Met1-Trp173 , Met1-Arg174 , Met1-Arg176 , Met1-Arg177 , or Met1-Arg184 from KAT1 was fused to DNA coding for PL gly using a two-step PCR approach (18 )
A series of S1-4-PL / PLgly fusion proteins in which Arg165 , Arg171 , Arg174 , Arg176 , or Arg177 in S4 was replaced by valine was constructed to eliminate single positive charges (Fig. 4 , A and B)
Single mutation of the negatively charged residues , Asp95 , Asp105 , and Asp141 , had a clear effect on KAT1 topology , whereas single mutation of the positively charged residues , Arg165 , Arg171 , Arg174 , Arg176 , and Arg177 , did not
Arg176 , Arg177 , and / or Arg184 also contribute in stabilizing S4 in the membrane
Arg174 , Arg176 , Arg177 , and / or Arg184 helped stabilize S4 in the membrane at the end of the S4 insertion event (Fig. 5 )

R176V

We therefore measured K + currents of full-length KAT1 containing these same mutations to evaluate the effect of the mutations on K + channel function and found that R174V , R176V , and R177V had the channel activity , although the voltage dependence of current amplitude of R176V and R177V differed from that of the wild-type (Fig. 4 C)
B , membrane topology of the R165V , R171V , R174V , R176V , or R177V mutants
K + current was detected (+) in the R174V- , R176V- , or R177V-expressing oocytes but not detected (ND) in the D95V- , D105V- , D141V- , R165V- or R171V-expressing oocytes

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