title: Crystallization and preliminary X-ray diffraction analysis of tau protein microtubule-binding motifs in complex with Tau5 and DC25 antibody Fab fragments.
abstract: The Alzheimer's disease-associated protein tau is an intrinsically disordered protein with no preferred structure in solution. Under physiological conditions, tau binds to microtubules and regulates their dynamics, whereas during the development of neurodegeneration tau dissociates from microtubules, misfolds and creates highly insoluble deposits. To elucidate the determinants of tau-protein misfolding, tau peptides from microtubule-binding motifs were crystallized in complexes with Fab fragments of specific monoclonal antibodies. The crystals diffracted to 1.69 Å resolution and gave complete data sets using a synchrotron X-ray source. Molecular replacement was used to solve the phase problem.
authors.affiliation: Institute of Neuroimmunology, Slovak Academy of Sciences, Dubravska cesta 9, 84510 Bratislava, Slovakia.
authors.forename: Ondrej
authors.initials: O
authors.lastname: Cehlar
authors.forename: Rostislav
authors.initials: R
authors.lastname: Skrabana
authors.forename: Andrej
authors.initials: A
authors.lastname: Kovac
authors.forename: Branislav
authors.initials: B
authors.lastname: Kovacech
authors.forename: Michal
authors.initials: M
authors.lastname: Novak
mesh_terms: D020816:Amino Acid Motifs; D000911:Antibodies, Monoclonal; D003460:Crystallization; D018360:Crystallography, X-Ray; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry* / Q000276:immunology; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D016875:tau Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D016875:tau Proteins