Structure solution of misfolded conformations adopted by intrinsically disordered Alzheimer's tau protein.
Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimer's paired helical filaments as neither of them could have been prepared in the form amenable to X-ray or NMR techniques. Using IDP tau property to attain regular tertiary structure after binding events during self-assembly or when complexed with its target we propose monoclonal antibodies as surrogate tau protein binding partners to form complexes and crystals for structure solution by X-ray technique.
Sevcik
Jozef
J
Institute of Neuroimmunology, Slovak Academy of Sciences, Dubravska cesta 9, 845 10 Bratislava, Slovakia.
Skrabana
Rostislav
R
Kontsekova
Eva
E
Novak
Michal
M
D000911:Antibodies, Monoclonal; D011487:Protein Conformation; D017510:Protein Folding; D016875:tau Proteins / Q000737:chemistry* / Q000276:immunology
D000911:Antibodies, Monoclonal; D016875:tau Proteins