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Structure Solution of Misfolded Conformations Adopted by Intrinsically Disordered Alzheimer's Tau Protein

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Abstract:

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 Xray or NMR techniques. Using IDP tau property to attain regular tertiary structure after binding events during selfassembly 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.





Keywords: Alzheimer's disease; crystal structure; intrinsically disordered protein; monoclonal antibody; tau protein

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986609787049349

Publication date: January 1, 2009

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2009/00000016/00000001/art00010
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