Yang J M, Yoneda K, Morita E, Imamura S, Nam K, Lee E S, Steinert P M
Department of Dermatology, College of Medicine, Sung Kyun Kwan University, Seoul, Korea.
J Invest Dermatol. 1997 Nov;109(5):692-4. doi: 10.1111/1523-1747.ep12338320.
We report a mutation in a case of epidermolytic hyperkeratosis that results in a proline for alanine substitution in the residue position 12 of the 1A subdomain of the keratin 10 chain (codon 158). The disease phenotype is consistent with the inappropriate substitution of a proline near the beginning of the rod domain, because it is likely to seriously disrupt the structural organization of coiled-coil molecules within keratin intermediate filaments. Mutations/substitutions in this position have not been reported in any keratin disease. Position 12 is an alanine in all intermediate filament chains, and lies in the outer b heptad position of the coiled-coil. In vitro peptide interference assembly assays revealed that substitutions that alter residue size or charge at this position primarily interfere with keratin filament elongation.
我们报告了一例表皮松解性角化过度病例中的一种突变，该突变导致角蛋白10链1A亚结构域第12位残基（密码子158）处的丙氨酸被脯氨酸取代。该疾病表型与杆状结构域起始附近脯氨酸的不适当取代一致，因为这可能会严重破坏角蛋白中间丝内卷曲螺旋分子的结构组织。在任何角蛋白疾病中均未报道过该位置的突变/取代。在所有中间丝链中，第12位都是丙氨酸，位于卷曲螺旋的外部b七肽位置。体外肽干扰组装试验表明，在此位置改变残基大小或电荷的取代主要干扰角蛋白丝的伸长。
