| Title: | Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1024586 |
| landingPage: |
http://www.iedb.org/assay/1945051 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
2012
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Clare Peters-Libeu
Jason Miller
Earl Rutenber
Yvonne Newhouse
Preethi Krishnan
Kenneth Cheung
Danny Hatters
Elizabeth Brooks
Kartika Widjaja
Tina Tran
Siddhartha Mitra
Montserrat Arrasate
Luis A Mosquera
Dean Taylor
Karl H Weisgraber
Steven Finkbeiner
|
| method: |
biological activity
|
| name: |
Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure.
|
| description: |
Small-angle X-ray scattering was used to determined the shape of htt fragments in complex with epitope-reactive 3B5H10 Fab. Htt fragments with 39 or 46 polyQ stretches were expressed within six fusion proteins to prevent aggregation and verify the results. The results show that in the complex, the htt fragment bends in the polyQ region and the polyQ epitope is cylindrical, 24 Å in diameter and 40-55 Å long. The authors conclude that the shape is consistent with a two-stranded hairpin structure with 16-24 Glu residues in contact with the paratope of the Fab and a turn of 4-8 Glu residues.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |