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PMID:3453101
| Citation |
McKeon, FD, Kirschner, MW and Caput, D Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319:463-8 |
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| 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. |
| Links |
PubMed Online version:10.1038/319463a0 |
| Keywords |
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 |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
part_of |
GO:0005635: nuclear envelope |
ECO:0000304: author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0005198: structural molecule activity |
ECO:0000304: author statement supported by traceable reference used in manual assertion |
|
F |
Seeded From UniProt |
complete | ||
See also
References
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