A premature stop codon mutation in the 2B helix termination peptide of keratin 5 in a German epidermolysis bullosa simplex Dowling-Meara case.

Abstract

Epidermolysis bullosa simplex (EBS) is caused by defective assembly of keratin intermediate filaments in basal keratinocytes and recent studies indicated causal mutations in the keratin KRT5 and KRT14 genes. In this study, we describe a novel KRT5 mutation in a German sporadic case of EBS Dowling-Meara. Transition of G to T (nucleotide position 2334) leads to a premature stop codon (E477stop, residue 93 of the 2B helix) in the last residue of the highly conserved helix-termination peptide K/LLEGE of the 2B rod domain of keratin K5. This represents the first premature stop codon mutation identified within the K/LLEGE motif of any disorder reported so far that is caused by keratin mutations.

• Authors: F B Müller, I Anton-Lamprecht, W Küster, B P Korge
• Journal: The Journal of investigative dermatology (J Invest Dermatol) Vol. 112 Issue 6 Pg. 988-90 (Jun 1999) ISSN: 0022-202X [Print] United States
• PMID: 10383750 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Codon, Terminator
• Peptide Termination Factors
• Keratins

Topics

• Adult
• Codon, Terminator (genetics)
• Epidermolysis Bullosa Simplex (genetics)
• Female
• Humans
• Keratins (chemistry, genetics)
• Pedigree
• Peptide Termination Factors (chemistry, genetics)
• Point Mutation
• Protein Structure, Tertiary
• Skin (ultrastructure)