Mutations in X-linked ichthyosis disrupt the active site structure of estrone/DHEA sulfatase

Biochim Biophys Acta. 2004 Dec 24;1739(1):1-4. doi: 10.1016/j.bbadis.2004.09.003.

Abstract

X-linked ichthyosis is an inherited genetic disorder of the skin that results from steroid sulfatase (STS) deficiency. Seven critical point mutations have been previously reported for the STS gene, six leading to amino acid substitutions and one to a premature termination of the polypeptide chain. The three-dimensional structure of the full-length human enzyme has been recently determined. Amino acid substitutions due to point mutations in X-linked ichthyosis are mapped onto the three-dimensional structure of human STS. In each case, the substitution appears to cause disruption of the active site architecture or to interfere with the enzyme's putative membrane-associating motifs crucial to the integrity of the catalytic cleft, thereby providing an explanation for the loss of STS activity.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Substitution
  • Binding Sites
  • Humans
  • Ichthyosis, X-Linked / genetics*
  • Models, Molecular
  • Point Mutation*
  • Protein Conformation
  • Steryl-Sulfatase / chemistry
  • Steryl-Sulfatase / genetics*
  • Steryl-Sulfatase / metabolism*

Substances

  • Steryl-Sulfatase