Journal Article
Research Support, U.S. Gov't, P.H.S.
Add like
Add dislike
Add to saved papers

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

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.

Full text links

We have located links that may give you full text access.
Can't access the paper?
Try logging in through your university/institutional subscription. For a smoother one-click institutional access experience, please use our mobile app.

Related Resources

For the best experience, use the Read mobile app

Mobile app image

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app

All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.

By using this service, you agree to our terms of use and privacy policy.

Your Privacy Choices Toggle icon

You can now claim free CME credits for this literature searchClaim now

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app