3OVJ
Structure of an amyloid forming peptide KLVFFA from amyloid beta in complex with orange G
Summary for 3OVJ
| Entry DOI | 10.2210/pdb3ovj/pdb |
| Related | 3OW9 |
| Descriptor | KLVFFA hexapeptide segment from Amyloid beta, 7-hydroxy-8-[(E)-phenyldiazenyl]naphthalene-1,3-disulfonic acid (3 entities in total) |
| Functional Keywords | amyloid-like protofibril, protein fibril |
| Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
| Total number of polymer chains | 4 |
| Total formula weight | 3716.45 |
| Authors | Landau, M.,Eisenberg, D. (deposition date: 2010-09-16, release date: 2011-07-06, Last modification date: 2024-02-21) |
| Primary citation | Landau, M.,Sawaya, M.R.,Faull, K.F.,Laganowsky, A.,Jiang, L.,Sievers, S.A.,Liu, J.,Barrio, J.R.,Eisenberg, D. Towards a pharmacophore for amyloid. Plos Biol., 9:e1001080-e1001080, 2011 Cited by PubMed Abstract: Diagnosing and treating Alzheimer's and other diseases associated with amyloid fibers remains a great challenge despite intensive research. To aid in this effort, we present atomic structures of fiber-forming segments of proteins involved in Alzheimer's disease in complex with small molecule binders, determined by X-ray microcrystallography. The fiber-like complexes consist of pairs of β-sheets, with small molecules binding between the sheets, roughly parallel to the fiber axis. The structures suggest that apolar molecules drift along the fiber, consistent with the observation of nonspecific binding to a variety of amyloid proteins. In contrast, negatively charged orange-G binds specifically to lysine side chains of adjacent sheets. These structures provide molecular frameworks for the design of diagnostics and drugs for protein aggregation diseases. PubMed: 21695112DOI: 10.1371/journal.pbio.1001080 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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