Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments

Peter M. Steinert, Robert H. Rice, Dennis R. Roop, Benes L. Trus, Alasdair C. Steven

Research output: Contribution to journalArticle

196 Scopus citations

Abstract

We have determined the complete primary structure of an intermediate filament subunit, the 59,000 molecular weight subunit of mouse epidermal keratin, from the nucleotide sequence of cDNA clones. The central portion of the sequence forms extended tracts of a coiled-coil α-helical conformation. This is flanked at both termini by similar non-α-helical sequences that are extremely rich in glycine residues, frequently configured in tandem peptide repeats. Limited chymotryptic digestion of keratin filaments containing this protein suggests a structural organization whereby the terminal glycine-rich sequences protrude from a conserved core structure into which the coiled-coil α-helical segments are packed.

Original languageEnglish (US)
Pages (from-to)794-800
Number of pages7
JournalNature
Volume302
Issue number5911
DOIs
StatePublished - 1983
Externally publishedYes

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