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-Structure paper
Title | Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure. |
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Journal, issue, pages | J. Mol. Biol., Vol. 421, Page 587-600, Year 2012 |
Publish date | May 31, 2011 (structure data deposition date) |
Authors | Peters-Libeu, C. / Miller, J. / Rutenber, E. / Newhouse, Y. / Krishnan, P. / Cheung, K. / Hatters, D. / Brooks, E. / Widjaja, K. / Tran, T. ...Peters-Libeu, C. / Miller, J. / Rutenber, E. / Newhouse, Y. / Krishnan, P. / Cheung, K. / Hatters, D. / Brooks, E. / Widjaja, K. / Tran, T. / Mitra, S. / Arrasate, M. / Mosquera, L.A. / Taylor, D. / Weisgraber, K.H. / Finkbeiner, S. |
External links | J. Mol. Biol. / PubMed:22306738 |
Methods | X-ray diffraction |
Resolution | 1.9 - 1.94 Å |
Structure data | PDB-3s96: PDB-4dcq: |
Chemicals | ChemComp-HOH: ChemComp-EDO: |
Source |
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Keywords | IMMUNE SYSTEM / FAB / huntingtin / Fab fragment / immunoglobulin domain / anti-polyglutamine / polyglutamine repeats |