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 R19Q 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 R19Q in KCMB2_RAT

Point mutation:	R19Q
Domain:	N-term
General numbering (KChannelDB):	-
Protein:	KCMB2_RAT (Kcnmb)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in KCMB2_RAT
Family alignments	Potassium channel beta subunits K(VCa)beta
Other point mutations / same position
Reference:	Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues. Xia XM, Ding JP, Lingle CJ J Gen Physiol 2003 Feb;121(2):125-48.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

R19Q

Currents resulting from a construct with neutralization of the first four positive charges in the NH2 terminus (R8QR14QK18QR19Q) are shown in Fig. 12 B
The absence of a major role of positively charged residues in the inactivation process is most dramatically illustrated with a construct in which all positive charges up through residue K41 (R8QR14QK18QR19QK24QR26QK33QR34QK35QK41Q) were neutralized
In B , currents resulted from construct R8QR14QK18QR19Q
In C , currents are from construct R8Q R14QK18QR19QK24QR26QK35QK41Q ; in D , D16RE17K ; in E , neutralization of all charge in first 26 amino acids , R8QR14QK18QR19QK24QR26QD16NE17Q
In G , currents resulted from mutation of R8QR14QK18QR19Q in a background of {Delta}FI ; in H , {Delta}FI-R8QR14QK18QR19QK24QR26QK35QK41Q ; in I , {Delta}FI-D16RE17K ; in J , {Delta}FI-R8QR14QK18QR19QK24QR26QD16NE17Q
Thus , for construct R8Q14Q K18QR19QD16NE17Q , all charges in the first 23 amino acids and , for construct R8Q14Q K18QR19QK24QR26QD16NE17Q , all charges in the first 26 amino acids of the NH2 terminus have been removed
For both cases , currents were remarkably comparable to wild-type alpha + ß2 currents (Fig. 12 E for R8QR14QK18QR19QK24QR26QD16NE17Q) with both {tau}on and {tau}off being somewhat more rapid than for alpha + ß2 currents (Table IV )
Furthermore , whereas neutralization of 3 positively charged residues in the Shaker NH2 terminus (R17QK18QK19Q) resulted in a 6.6-fold slowing of the inactivation rate (Murrell-Lagnado and Aldrich , 1993b(image) ) , neutralization of 4 positively charged residues (R9Q , R14Q , K18Q , R19Q) in the BK ß2 NH2 terminus resulted in a 1.6-fold increase in the inactivation rate (Table IV )
Neutralization of positively charged residues resulted in only small changes in {tau}on , as illustrated for {Delta}FI-R8QR14QK18QR19Q (Fig. 12 G) and for {Delta}FI-R8QR14QK18QR19QK24QR26QK33QR34QK35QK41Q (Fig. 12 H)

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