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 Q171R 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 Q171R in PRIO_OVICA

Point mutation:	Q171R
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_OVICA (PRNP,PRP)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in PRIO_OVICA
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 168 in Mammalian prion proteins family Position 168 in Prion proteins (PRP, PRNP) family
Reference:	Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants. Eghiaian F, Grosclaude J, Lesceu S, Debey P, Doublet B, Treguer E, Rezaei H, Knossow M Proc Natl Acad Sci U S A 2004 Jul 13;101(28):10254-9. Epub 2004 Jul 6.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

Q171R

Indeed , it was shown recently that ovine (Ov)PrP mutations V136A and Q171R , associated with a resistant phenotype in sheep , destabilize the recombinant prion protein (8 )
The crystal structure of the OvPrP ARQ variant allows us to localize the side chains of the amino acids associated with these polymorphisms ; together with the structures of the VRQ and ARR variants , it provides an opportunity to analyze the consequences of the A136V and Q171R sensitivity-modulating mutations in atomic detail
(Lower) Q171R
Structural comparisons of OvPrP variants ARR , ARQ , and VRQ show that mutations V136A and Q171R lead to disruption of hydrogen bonds located at the surface of the ovine recombinant prion protein
The measured unfolding free-enthalpy variations caused by the A136V and Q171R mutations (8 ) , -5.9 kJ / mol and 4.9 kJ / mol , respectively , are within the range of those observed when a hydrogen bond is gained or lost in a protein , provided there is no unpaired buried ion formed (28 )
In the particular case of the ARR variant , a combination of increased protease sensitivity and slower amyloidogenesis would account for a switch from scrapie susceptibility to resistance associated with the single Q171R substitution

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