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 E200K 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 E200K in PRIO_HUMAN

Point mutation:	E200K
Cited point mutation:	Glu200Lys,Glu-200-Lys
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_HUMAN (PRNP)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 200 in PRIO_HUMAN
Other point mutations / same protein	List of mutations in PRIO_HUMAN
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 200 in Mammalian prion proteins family Position 200 in Prion proteins (PRP, PRNP) family
Reference:	The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C). Thompson AJ, Barnham KJ, Norton RS, Barrow CJ Biochim Biophys Acta 2001 Jan 12;1544(1-2):242-54.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

Glu-200-Lys

Interestingly , Glu-200-Lys is a pathogenic mutation responsible for a familial form of TSE
The importance of Glu-200 for small alpha , Greek-helical formation in this region indicates that a Glu-200-Lys mutation could promote PrPSc formation through influencing local helical propensity

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