A novel glutamic acid to aspartic acid mutation near the end of the 2B rod domain in the keratin 1 chain in epidermolytic hyperkeratosis

被引：21

作者：

Yang, JM

Nam, K

Kim, HC

Lee, JH

Park, JK

Wu, K

Lee, ES

Steinert, PM

机构：

[1] Sungkyunkwan Univ, Sch Med, Samsung Med Ctr, Dept Dermatol,Kangnam Ku, Seoul 135710, South Korea

[2] Sungkyunkwan Univ, Samsung Biomed Res Inst, Clin Res Ctr, Sch Med, Seoul, South Korea

[3] Chungnam Natl Univ, Coll Med, Dept Dermatol, Taejon, South Korea

[4] NIAMSD, Skin Biol Lab, NIH, Bethesda, MD USA

来源：

JOURNAL OF INVESTIGATIVE DERMATOLOGY | 1999年 / 112卷 / 03期

关键词：

epidermolytic hyperkeratosis; glutamic acid; keratin;

D O I：

10.1038/sj.jid.5600439

中图分类号：

R75 [皮肤病学与性病学];

学科分类号：

100206 ;

摘要：

We report a mutation in a mild case of epidermolytic hyperkeratosis that results in a glutamic acid to aspartic acid substitution in a novel location, codon 477 or position 106 of the 2B rod domain of the keratin 1 chain. This residue has been conserved in all intermediate filament chains and lies near the beginning of the highly conserved helix termination sequence and just prior to the predicted molecular overlap region. Keratin filaments assembled in vitro from chains bearing this substitution are abnormal, indicating that the glutamic acid residue is critically involved in ionic interactions in intermediate levels of filament structure.

引用

页码：376 / 379

页数：4

共 16 条

[1] A highly conserved lysine residue on the head domain of type II keratins is essential for the attachment of keratin intermediate filaments to the cornified cell envelope through isopeptide crosslinking by transglutaminases [J].