Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
FD McKeon, MW Kirschner, D Caput - Nature, 1986 - nature.com
FD McKeon, MW Kirschner, D Caput
Nature, 1986•nature.comAbstract The A, B and C lamins are the major proteins of the nuclear envelope. The
complete nucleotide sequence of the coding region of the A and C lamins shows that these
proteins are identical except for their carboxy termini. The most prominent structural feature
of both lamins is an α-helical region of repeating heptads of amino acids that shows striking
homology with the entire family of cytoplasmic intermediate filament proteins. These features
suggest that the nuclear envelope is made up of a network of coiled-coil polymers.
complete nucleotide sequence of the coding region of the A and C lamins shows that these
proteins are identical except for their carboxy termini. The most prominent structural feature
of both lamins is an α-helical region of repeating heptads of amino acids that shows striking
homology with the entire family of cytoplasmic intermediate filament proteins. These features
suggest that the nuclear envelope is made up of a network of coiled-coil polymers.
Abstract
The A, B and C lamins are the major proteins of the nuclear envelope. The complete nucleotide sequence of the coding region of the A and C lamins shows that these proteins are identical except for their carboxy termini. The most prominent structural feature of both lamins is an α-helical region of repeating heptads of amino acids that shows striking homology with the entire family of cytoplasmic intermediate filament proteins. These features suggest that the nuclear envelope is made up of a network of coiled-coil polymers.
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