The juvenile microtubule-associated protein MAP2c is a rod-like molecule that forms antiparallel dimers.
We have developed a procedure to isolate the microtubule-associated protein 2c (MAP2c), a juvenile form of MAP2 occurring in mammalian brain. The shape, size, self-association, and antibody interactions of MAP2c were studied. Monomeric MAP2c is an elongated molecule with a length approximately 48 nm, considerably shorter than the higher molecular weight forms MAP2a or b of adult brain. Two monoclonal antibodies whose epitopes are near the N or C terminus, respectively, are located close to the opposite ends of the MAP2c rods. This places constraints on the types of internal folding of the molecule. MAP2c self-associates into dimers and fibrous aggregates. The dimers are predominantly antiparallel and nearly in register, as judged by antibody labeling.
Wille
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Max-Planck-Unit for Structural Molecular Biology, Deutsches Elektronen Synchrotron, Hamburg, Germany.
Mandelkow
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Mandelkow
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D000818:Animals; D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011487:Protein Conformation; D013552:Swine
D000911:Antibodies, Monoclonal; D000939:Epitopes; D008869:Microtubule-Associated Proteins