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pubmed-article:1375231pubmed:abstractTextWe 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.lld:pubmed
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pubmed-article:1375231pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1375231pubmed:articleTitleThe juvenile microtubule-associated protein MAP2c is a rod-like molecule that forms antiparallel dimers.lld:pubmed
pubmed-article:1375231pubmed:affiliationMax-Planck-Unit for Structural Molecular Biology, Deutsches Elektronen Synchrotron, Hamburg, Germany.lld:pubmed
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pubmed-article:1375231pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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