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 P475A 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 P475A in AKT6_ARATH

Point mutation:	P475A
Domain:	C-term
General numbering (KChannelDB):	-
Protein:	AKT6_ARATH (AKT6,SPIK,At2g2560)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 475 in AKT6_ARATH
Other point mutations / same protein	List of mutations in AKT6_ARATH
Family alignments	AKT-like Inward rectifiers 6TMs Plant potassium channels
Other point mutations / same position	Position 458 in AKT-like Inward rectifiers 6TMs family Position 458 in Plant potassium channels family
Reference:	Scanning the intracellular S6 activation gate in the shaker K+ channel. Hackos DH, Chang TH, Swartz KJ J Gen Physiol 2002 Jun;119(6):521-32.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

P475A

For P475A , holding voltage was -100 mV and depolarizations were from -100 to 0 mV , in 10-mV increments
Smooth curves are single Boltzmann fits to the data with parameters as follows: W434F: V50 = -47.1 mV , z = 4.1 ; P473W: V50 = -64.1 mV , z = 2.5 ; P473A: V50 = -55.9 mV , z = 7.0 ; V478W: V50 = -48.6 mV , z = 4.1 ; P475A: V50 = -41.1 mV , z = 1.7
Gating currents obtained for W434F , a previously described nonconducting mutant (Perozo et al. , 1993(image) ) , are shown in Fig. 3 along with gating currents for V478W , P473A , P473W , and P475A
For P473A and P473W , the Q-V relations are shifted to negative voltages , whereas in the case of P475A , the Q-V is shifted to positive voltages
For example , three mutants in this motif (P473D , V474D / W) result in retention of the protein in the endoplasmic reticulum and three other mutants (P473A , P473W , and P475A) result in nonconducting channels where the Q-V relations are significantly different than the control channel
Although it seems unlikely that the gate has been directly plugged by the substituted residue because mutations to both smaller (P473A , P475A) and larger (P473W) side chains gives rise to similar phenotypes , it is possible that the structure of a nearby occluding region has been rendered nonconducting by propagated structural changes

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