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_MOUSE at position 209 were found are listed after the table.
| Protein | PRIO_MOUSE (P04925) Gene: Prnp,Prn-p (other point mutations) | Swiss-Prot
Cross-reference table
Family page |
| Position | V209 | |
| General numbering (PrionDB) | - |
| Domain | Not determined |
| Family alignments |
Mammalian prion proteins
Prion proteins (PRP, PRNP)
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| Other point mutations at the same position |
Position 210 in Mammalian prion proteins family
Position 210 in Prion proteins (PRP, PRNP) family
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| Reference #1 | Liemann S, Glockshuber R
Biochemistry 1999 Mar 16;38(11):3258-67. | Medline |
| Text source | HTML and PDF full texts |
| Point mutation | V209I (True positive) | |
| Cited point mutation | V210I,Val210Ile | |
| Reference #2 | Stewart RS, Harris DA
J Biol Chem 2001 Jan 19;276(3):2212-20. | Medline |
| Text source | HTML full text |
| Point mutation | V209I (True positive) | |
Reference #2 (Stewart RS et al.): V209I
- The following mutations were introduced into the wild-type PrP cDNA using polymerase chain reaction as described previously (14 ): PG11 (six-octapeptide insertion) , PG14 (eight-octapeptide insertion) , K109I / H110I , 3AV (Ala --> Val at 112 , 114 , and 117) , A116V , D177N , V179I , F197S , E199K , and V209I
- The human homologues of the mutations are associated with the following familial prion diseases: Creutzfeldt-Jakob disease (PG11 , PG14 , V179I , E199K , V209I) , Gerstmann-Sträussler syndrome (A116V , F197S) , and fatal familial insomnia (D177N)
- However , five of the pathogenic PrPs (PG11 , PG14 , D177N , F197S , and E199K) do in fact assume a protease-resistant form that resembles PrP Sc when expressed in transfected CHO and BHK cells (2 , 23 ) , 2 while three of mutants (A116V , V179I , and V209I) are protease-sensitive and display other properties characteristic of PrPC.3 This comparison makes it clear that there is no correlation between the efficiency with which a mutation promotes conversion to a PrP Sc-like state in cell culture and its potency in inducing CtmPrP
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Reference #1 (Liemann S et al.): 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 ± 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)
- 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)
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Reference #1 (Liemann S et al.): 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)
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2005, PrionDB.
cmbi.ru.nl), 22-Aug-2005