Crystal Structure-Based Analysis of Human Glucuronyltransferase 1

Lars C. Pedersen, Thomas A. Darden, Yoshimitsu Kakuta, Masahiko Negishi

Research output: Contribution to journalReview articlepeer-review

Abstract

Glucuronyltransferase I (GlcAT-I) is a key enzyme in heparan/chondroitin biosynthesis (1). The X-ray crystal structure of human GlcAT-1 has been solved in the presence of both UDP and substrate analog. The structure reveals a two sub-domain structure known as the SGC domain. Donor substrate-binding site resides in the N-terminal sub-domain, while acceptor substrate-binding site is located in the C-terminal sub-domain. In addition to conserved residues responsible for the donor binding, various residues that interact with the acceptor molecule have now been identified. The GlcAT-1 provides the structural basis for understanding the structure and function of glycosyltransferases.

Original languageEnglish
Pages (from-to)121-129
Number of pages9
JournalTrends in Glycoscience and Glycotechnology
Volume13
Issue number70
DOIs
Publication statusPublished - Jan 1 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Organic Chemistry

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