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 T188A 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 T188A in Q8FHW6_ECOL6

Point mutation:	T188A
Cited point mutation:	Thr188Ala,Thr-188
Domain:	Loop 5-6
General numbering (KChannelDB):	-
Protein:	Q8FHW6_ECOL6 (kch,c171)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 188 in Q8FHW6_ECOL6
Other point mutations / same protein	List of mutations in Q8FHW6_ECOL6
Family alignments	KCH 6TMs Archaea and Bacteria potassium channels
Other point mutations / same position	Position 182 in KCH 6TMs family Position 182 in Archaea and Bacteria potassium channels family
Reference:	Identification of essential residues involved in the glutamate binding pocket of the group II metabotropic glutamate receptor. Malherbe P, Knoflach F, Broger C, Ohresser S, Kratzeisen C, Adam G, Stadler H, Kemp JA, Mutel V Mol Pharmacol 2001 Nov;60(5):944-54.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

Thr-188

Furthermore , mutagenesis studies verified that two residues , Ser-165 and Thr-188 of mGlu1 , were indeed crucial for binding to glutamate and quisqualate as predicted by this model (O'Hara et al. , 1993(image) )
Because the Ser-165 and Thr-188 of mGlu1 receptor have been shown previously to be crucial for the binding to glutamate , our mutated residues were chosen from two regions proximal to these residues (Fig. 1 )
In an earlier study (O'Hara et al. , 1993(image) ) , it was demonstrated that the conversion of Ser-165 and Thr-188 of mGlu1 receptor (Ser-145 and Thr-168 in mGlu2) into alanine decreased the glutamate potency by 100- and 10 , 000-fold , respectively
Among the residues shown in the mGlu1 crystal structure to interact directly and / or via a water molecule with glutamate , Arg-78 , Ser-165 , Thr-188 , Asp-208 , Tyr-236 , and Asp-318 (Arg-61 , Ser-145 , Thr-168 , Asp-188 , Tyr-216 , and Asp-295 , respectively , in mGlu2) are identical in all mGlu receptors

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