| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1025355 |
| landingPage: |
http://www.iedb.org/assay/1970426 |
| type: |
Literature
|
| publicationVenue: |
Endocrinology
|
| dates: |
2013
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Sepehr Hamidi
Chun-Rong Chen
Ramachandran Murali
Sandra M McLachlan
Basil Rapoport
|
| method: |
ELISA
|
| name: |
Probing structural variability at the N terminus of the TSH receptor with a murine monoclonal antibody that distinguishes between two receptor conformational forms.
|
| description: |
The epitope was deduced.
The mAbs bound two overlapping peptides (MGCSSPPCECHQEEDFRVTCK and ECHQEEDFRVTCKDIQRIPS) that share the epitope. Alanine substitutions of TSHR loop2 residues E34, E35, and D36 severely diminished binding of mAb 3BD10 and a lower effect was found for substitution of residues F37 and V39. For 3E5 the substitution of residues E35, D36 and F37 had a strong effect on recognition and lower effect was seen for substitution of E34 and V39. The region CSSPPC, corresponding to loop 1, was found not to affect binding to the peptides in ELISA by mutation analysis.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |