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
|Cited point mutation:||Arg176Val,Arg176|
|General numbering (KChannelDB):|| 455|
|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|
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.
|Other point mutations / same article||List|
|Text source||HTML full text|
|Validation status||Not yet checked|
- 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 )
- 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