Abstract
Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimers 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, tau protein, intrinsically disordered protein, monoclonal antibody, crystal structure
Protein & Peptide Letters
Title: Structure Solution of Misfolded Conformations Adopted by Intrinsically Disordered Alzheimers Tau Protein
Volume: 16 Issue: 1
Author(s): Jozef Sevcik, Rostislav Skrabana, Eva Kontsekova and Michal Novak
Affiliation:
Keywords: Alzheimer's disease, tau protein, intrinsically disordered protein, monoclonal antibody, crystal structure
Abstract: Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimers 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.
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Cite this article as:
Sevcik Jozef, Skrabana Rostislav, Kontsekova Eva and Novak Michal, Structure Solution of Misfolded Conformations Adopted by Intrinsically Disordered Alzheimers Tau Protein, Protein & Peptide Letters 2009; 16 (1) . https://dx.doi.org/10.2174/092986609787049349
DOI https://dx.doi.org/10.2174/092986609787049349 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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