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 different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in PRIO_HUMAN at position 99 were found are listed after the table.

Point mutations at position W99 in PRIO_HUMAN

Protein	PRIO_HUMAN (P04156) Gene: PRNP (other point mutations)	Swiss-Prot Cross-reference table Family page
Position	W99
General numbering (PrionDB)	-
Domain	Not determined
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations at the same position	Position 99 in Mammalian prion proteins family Position 99 in Prion proteins (PRP, PRNP) family
Reference #1	Apetri AC, Surewicz WK J Biol Chem 2002 Nov 22;277(47):44589-92.	Medline
Text source	HTML and PDF full texts
Point mutation	W99F (True positive)
Cited point mutation	Trp99Phe,Trp99
Reference #2	Apetri AC, Surewicz K, Surewicz WK J Biol Chem 2004 Apr 23;279(17):18008-14. Epub 2004 Feb 2.	Medline
Text source	HTML full text
Point mutation	W99F (True positive)

Relevant sentences

Reference #1 (Apetri AC et al.): Trp99

This was accomplished by replacing Trp99 with Phe and , on that background , substituting Phe or Tyr at different positions with tryptophan
This was accomplished by replacing Trp99 with Phe and , on that back* This work was supported by National Institutes of Health Grant NS38604 (to W

Reference #2 (Apetri AC et al.): W99F

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)
alpha -Helices are shown in red ; the fluorescent probe Trp-218 is shown in green ; the position of the W99F substitution is represented as a black dot ; and the disulfide bond between Cys-179 and Cys-214 is indicated in yellow
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