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 Y218W 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 Y218W in PRIO_HUMAN

Point mutation:	Y218W
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_HUMAN (PRNP)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 218 in PRIO_HUMAN
Other point mutations / same protein	List of mutations in PRIO_HUMAN
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 218 in Mammalian prion proteins family Position 218 in Prion proteins (PRP, PRNP) family
Reference:	The effect of disease-associated mutations on the folding pathway of human prion protein. Apetri AC, Surewicz K, Surewicz WK J Biol Chem 2004 Apr 23;279(17):18008-14. Epub 2004 Feb 2.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	True positive

Relevant sentences:

Y218W

All variants containing mutations linked to familial prion diseases (P102L , D178N with 129M and 129V polymorphism , V180I , F198S , E200K , R208H , V210I , and Q217R) were constructed on the background of W99F / Y218W huPrP-(90-231) (21 ) by site-directed mutagenesis using appropriate primers and the QuikChange kit (Stratagene)
All these mutations were introduced on the background of an engineered single Trp variant Y218W / W99F of huPrP-(90-231)
Furthermore , the Y218W substitution does not significantly perturb the structure or thermodynamic stability of PrP (21 )
Equilibrium Unfolding Studies—Prior to kinetic stopped-flow experiments , the effect of individual disease-associated point mutations on the global thermodynamic stability of Y218W / W99F huPrP-(90-231) was probed by equilibrium unfolding in urea
These data show that whereas some of the disease-associated mutations produce a pronounced decrease in the global stability of Y218W / W99F huPrP-(90-231) , the effect of others (e.g. P102L and E200K) is essentially negligible
Most important , the destabilization induced by familial mutations found here for Y218W / W99F huPrP-(90-231) corresponds closely to the values reported in similar studies using unmodified mouse (28 ) or human prion proteins (29 )
The wild-type (WT) protein refers to W99F / Y218W huPrP-(90-231) in the absence of any disease-associated mutations
(image) 2 In the remainder of the text , the wild-type protein refers to W99F / Y218W huPrP-(90-231) in the absence of any disease-associated mutations

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