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Mapping the interaction site of prion protein and Sho
- Source :
- Molecular biology reports. 37(5)
- Publication Year :
- 2009
-
Abstract
- The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61-77 and PrP(C) 108-126 domains. This indicates that Sho may play a role in the physiological function of PrP(C) and prion pathogenesis.
- Subjects :
- Immunoprecipitation
Prions
animal diseases
Two-hybrid screening
education
Mutant
Nerve Tissue Proteins
Plasma protein binding
Biology
GPI-Linked Proteins
Pathogenesis
Mice
Protein structure
Two-Hybrid System Techniques
Protein Interaction Mapping
Genetics
Animals
Molecular Biology
Reproducibility of Results
General Medicine
Surface Plasmon Resonance
Yeast
nervous system diseases
Fungal prion
Protein Structure, Tertiary
Biochemistry
Protein Binding
Subjects
Details
- ISSN :
- 15734978
- Volume :
- 37
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Molecular biology reports
- Accession number :
- edsair.doi.dedup.....431e2277635120971b960d92e5b98b63