PrionDB: Extraction of mutation data from the literature

2005, PrionDB.

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 T198A 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 T198A in PRIO_MOUSE

Point mutation:	T198A
Cited point mutation:	T199A,Thr199Ala,Thr-199
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_MOUSE (Prnp,Prn-p)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 198 in PRIO_MOUSE
Other point mutations / same protein	List of mutations in PRIO_MOUSE
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 199 in Mammalian prion proteins family Position 199 in Prion proteins (PRP, PRNP) family
Reference:	Glycosylation of prions and its effects on protein conformation relevant to amino acid mutations. Wong NK, Renouf DV, Lehmann S, Hounsell EF J Mol Graph Model 2000 Apr;18(2):126-34, 163-5.	Medline
Other point mutations / same article	List
Text source	PDF full text
Validation status	True positive

Relevant sentences:

Thr-199

Residues involved in H-bonding to the glycan (mainly to the Fuc residue) include Thr-188 , Glu-196 , Thr-199 , Thr192 , and Val-189 , whereas residues involved in hydrophobic interaction include Gly-195 and Lys-194
To further support the effect of glycosylation on prion formation , Lehmann and Harris5 studied the role of N-glycans in determining the properties of PrP in which glycosylation has been blocked by replacement of Thr-183 and Thr-199 to Ala at one or both of the AsnXaaThr / Ser consensus sites
However , results indicate that PrP proteins mutated at Thr-183 alone or at both Thr-183 and Thr-199 fail to reach the cell surface after synthesis , and that those mutated at Thr-199 can be detected on the plasma membrane

F.Horn (priondbcmbi.ru.nl), 22-Aug-2005