PrionDB: Extraction of mutation data from the literature

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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 179 were found are listed after the table.

Point mutations at position C179 in PRIO_HUMAN

ProteinPRIO_HUMAN (P04156)    Gene: PRNP    (other point mutations)Swiss-Prot
Cross-reference table
Family page
PositionC179
General numbering (PrionDB) -
DomainNot determined
Family alignments Mammalian prion proteins
Prion proteins (PRP, PRNP)
Other point mutations at the same position Position 179 in Mammalian prion proteins family
Position 179 in Prion proteins (PRP, PRNP) family
Reference #1Capellari S, Zaidi SI, Urig CB, Perry G, Smith MA, Petersen RB
J Biol Chem 1999 Dec 3;274(49):34846-50.		Medline
Text sourceHTML full text
Point mutationC179A (True positive)
Reference #2Maiti NR, Surewicz WK
J Biol Chem 2001 Jan 26;276(4):2427-31.		Medline
Text sourceHTML full text
Point mutationC179A (True positive)
Reference #3Bosques CJ, Imperiali B
Proc Natl Acad Sci U S A 2003 Jun 24;100(13):7593-8.		Medline
Text sourceabstract
Point mutationC179S (True positive)

Relevant sentences

Reference #1 (Capellari S et al.): C179A
  • The constructs used in this study employed alanine replacement of cysteine at residue 179 alone (C179A (-Cys1)) , residue 214 alone (C214A (-Cys2)) , or residues 179 and 214 together (C179A / C214A (-Cys1+2)) (Fig. 2 A)

  • H , diglycosylated with highly modified glycans ; I , intermediate ; U , unglycosylated ; H imm , diglycosylated with immature glycans ; C , control cell line ; -Cys1 , C179A ; -Cys2 , C214A ; -Cys1+2 , C179A / C214A

  • The same result was obtained when we digested the C214A and C179A / C214A mutants (data not shown)

  • However , with mutant PrP and the same battery of antibodies , it was apparent that C179A mutant PrP was principally retained in complexes with PDI and calnexin , both at the initial time point and after the 2-h chase (Fig. 4 B)

  • In contrast , the double mutant (C179A / C214A) demonstrated a stable interaction principally with grp94 (Fig. 4 B)

  • However , a significant fraction of C179A / C214A reached the cell surface or was secreted

  • As demonstrated above , the C179A / C214A mutant reached the cell surface

Reference #2 (Maiti NR et al.): C179A
  • The C179A / C214A variant of huPrP23-231 was obtained by site-directed mutagenesis using the primers 5'-C TTT GTG CAC GAC GCC GTC AAT ATC AC and 5'-GT GAT ATT GAC GGC GTC GTG CAC AAA G for Cys179 --> Ala replacement and 5'-GTT GAG CAG ATG GCG ATC ACC CAG TAC and 5'-GTA CTG GGT GAT CGC CAT CTG CTC AAC for Cys214 --> Ala replacement

  • The C179A / C214A variant was expressed by the same procedure

  • The free peptide and thrombin were removed by selective precipitation of C179A / C214A huPrP23-231 in sodium phosphate buffer , pH 7.0

  • Very similar behavior was observed for prion protein variants in which the disulfide bridge was removed by a replacement of Cys residues with alanine (C179A / C214A huPrP23-231)

  • Far-UV circular dichroism spectra for the wild-type huPrP23-231 with native disulfide bridge (------) , reduced huPrP23-231 (- - -) , and the Cys-free (C179A / C214A) variant of huPrP23-231 (--- · · ---)

  • Near-UV circular dichroism spectra for the wild-type huPrP23-231 with native disulfide bridge (------) and the Cys-free (C179A / C214A) variant of huPrP23-231 (--- · · ---)

  • Fluorescence spectra of ANS alone (····) and in the presence of the wild-type huPrP23-231 with native disulfide bridge (------) , reduced huPrP23-231 (- - -) , and the Cys-free (C179A / C214A) variant of huPrP23-231 (--- · · ---)

  • Urea-induced unfolding of the wild-type huPrP23-231 with native disulfide bridge (triangle ) , reduced huPrP23-231 ((image)) , and the Cys-free (C179A / C214A) variant of huPrP23-231 (open circle )

  • Far-UV circular dichroism spectra of the reduced huPrP23-231 (A) and the Cys-free (C179A / C214A) variant of huPrP23-231 (B) in the absence (------) and presence (--- --- ---) of 50 mM NaCl

  • Size-exclusion chromatography profiles for of the wild-type huPrP23-231 with native disulfide bridge (top) , reduced huPrP23-231 (middle) and the Cys-free (C179A / C214A) variant of huPrP23-231 (bottom)

Reference #3 (Bosques CJ et al.): C179S
  • Further-more , the aggressive fibrillization of a C179S mutant of this fragment highlights the significant role of disulfide stability in retarding the rate of fibril formation

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