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PMID: 3453101 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins.

Nature ·Vol. 319 ·No. 6053 ·1986-00-00 ·Pages 463-8

McKeon FD, Kirschner MW, Caput D

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 alpha-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.

MeSH Terms
Amino Acid Sequence Base Sequence Cloning, Molecular DNA/analysis Humans Intermediate Filament Proteins/genetics Lamins Nucleoproteins/genetics Peptide Fragments/analysis Protein Conformation Sequence Homology, Nucleic Acid Structure-Activity Relationship
Chemicals
Intermediate Filament Proteins Lamins Nucleoproteins Peptide Fragments DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
McKeon F D
Kirschner M W
Caput D
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1986-00-00
Pages
463-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
GENBANK
X03444, X03445
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