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 language | English |
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Pages (from-to) | 121-129 |
Number of pages | 9 |
Journal | Trends in Glycoscience and Glycotechnology |
Volume | 13 |
Issue number | 70 |
DOIs | |
Publication status | Published - Mar 2001 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Organic Chemistry