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 V209I 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 V209I in PRIO_MOUSE

Point mutation:	V209I
Cited point mutation:	V210I,Val210Ile
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 209 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 210 in Mammalian prion proteins family Position 210 in Prion proteins (PRP, PRNP) family
Reference:	Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Liemann S, Glockshuber R Biochemistry 1999 Mar 16;38(11):3258-67.	Medline
Other point mutations / same article	List
Text source	HTML and PDF full texts
Validation status	True positive

Relevant sentences:

V210I

------------------------------------------------------------------------ Table 1: Thermodynamic Stabilities of mPrP(121-231) Variants , mPrP(121-231) Wild Type , and Full-Length mPrP(23-231) Wild Type at pH 7.0 and 25 (image)C mPrP protein prion disease phenotype (image)G(image) fold (kJ mol-1)a (image)(image)G(image) fold (variant - wild type) b cooperativity (kJ mol-1 M-1)a [urea]1 / 2 (M) a mPrP(121-231) wt -29.7 ą 1.0 4.8 ą 0.2 6.2 mPrP(23-231) wt -25.5 ą 1.0 4.2 ą 1.9 4.1 ą 0.2 6.3 M129V polymorphism (human) -28.2 ą 1.0 1.4 ą 2.0 4.5 ą 0.2 6.3 D178N / M129 FFI -22.5 ą 0.7 7.2 ą 1.7 4.7 ą 0.1 4.8 D178N / V129 CJD -21.7 ą 0.9 8.0 ą 1.8 4.5 ą 0.2 4.9 V180I GSS -27.6 ą 0.8 2.1 ą 1.7 4.5 ą 0.1 6.2 T183A CJD -10.4 ą 2.1 19.3 ą 3.1 3.5 ą 0.5 3.0 T190V polymorphism (mouse) -30.3 ą 1.5 -0.7 ą 2.4 4.8 ą 0.2 6.4 F198S GSS -19.4 ą 0.8 10.3 ą 1.7 4.4 ą 0.2 4.5 E200K CJD -29.1 ą 1.5 0.6 ą 2.4 4.9 ą 0.3 5.9 R208H CJD -23.7 ą 1.5 6.0 ą 2.5 4.3 ą 0.3 5.6 V210I CJD -28.6 ą 1.6 1.1 ą 2.6 4.5 ą 0.3 6.3 Q217R GSS -20.8 ą 0.8 8.9 ą 1.7 4.5 ą 0.2 4.7 a The thermodynamic stabilities were measured by urea-induced equilibrium transitions (Figure 5)
Table 1: Thermodynamic Stabilities of mPrP(121-231) Variants , mPrP(121-231) Wild Type , and Full-Length mPrP(23-231) Wild Type at pH 7.0 and 25 °C mPrP protein prion disease phenotype G°fold (kJ mol-1)a G°fold (variant - wild type)b cooperativity (kJ mol-1 M-1)a [urea]1 / 2 (M)a mPrP(121-231) wt - -29.7 ( 1.0 - 4.8 ( 0.2 6.2 mPrP(23-231) wt - -25.5 ( 1.0 4.2 ( 1.9 4.1 ( 0.2 6.3 M129V polymorphism (human) -28.2 ( 1.0 1.4 ( 2.0 4.5 ( 0.2 6.3 D178N / M129 FFI -22.5 ( 0.7 7.2 ( 1.7 4.7 ( 0.1 4.8 D178N / V129 CJD -21.7 ( 0.9 8.0 ( 1.8 4.5 ( 0.2 4.9 V180I GSS -27.6 ( 0.8 2.1 ( 1.7 4.5 ( 0.1 6.2 T183A CJD -10.4 ( 2.1 19.3 ( 3.1 3.5 ( 0.5 3.0 T190V polymorphism (mouse) -30.3 ( 1.5 -0.7 ( 2.4 4.8 ( 0.2 6.4 F198S GSS -19.4 ( 0.8 10.3 ( 1.7 4.4 ( 0.2 4.5 E200K CJD -29.1 ( 1.5 0.6 ( 2.4 4.9 ( 0.3 5.9 R208H CJD -23.7 ( 1.5 6.0 ( 2.5 4.3 ( 0.3 5.6 V210I CJD -28.6 ( 1.6 1.1 ( 2.6 4.5 ( 0.3 6.3 Q217R GSS -20.8 ( 0.8 8.9 ( 1.7 4.5 ( 0.2 4.7 a The thermodynamic stabilities were measured by urea-induced equilibrium transitions (Figure 5)

Val210Ile

Lane 1 , molecular mass standards ; 2 , wild-type mPrP(121-231) before induction with IPTG ; 3 , wild-type mPrP(121-231) 18 h after induction (same as for the variants shown in the following lanes) ; 4 , Met129Val ; 5 , Met129 / Asp178Asn ; 6 , Met129Val / Asp178Asn ; 7 , Val180Ile ; 8 , Thr183Ala ; 9 , Thr190Val ; 10 , Phe198Ser ; 11 , Glu200Lys ; 12 , Arg208His ; 13 , Val210Ile ; 14 , Gln217Arg
Like mPrP(121-231) wild type (37) , the TSE-related variants Val180Ile , Glu200Lys , Arg208His , and Val210Ile as well the polymorphism variants Met129Val and Thr190Val were produced as soluble proteins in the periplasm of E
Both polymorphism variants Met129Val and Thr190Val as well as the TSE-related variants Glu200Lys and Val210Ile have the same stability as mPrP(121-231) wild type within experimental error ((image)G(image)fold ~ -29 kJ mol-1 ; Table 1)
The valine side chains at positions 180 and 210 both contribute to the hydrophobic protein core , but their replacement by the bulkier isoleucine side chains in the variants Val180Ile and Val210Ile barely affects the stability of mPrP(121-231)
For example , the observation that the amino acid replacement Val210Ile has no effect on the intrinsic stability of mPrP(121-231) suggests similar tendencies of wild type and mutant PrP C to be converted into PrP Sc (89) , but in case of the exchange Glu200Lys , which does not affect the stability either , only the mutant PrP is converted into the protease-resistant form (87)
Both polymorphism variants Met129Val and Thr190Val as well as the TSE-related variants Glu200Lys and Val210Ile have the same stability as mPrP(121-231) wild type within experimental error ( G°fold -29 kJ mol-1 ; Table 1)

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