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Structural insight into mammalian sialyltransferases.

Authors :
Rao, Francesco V.
Rich, Jamie R.
Rakić, Bojana
Buddai, Sai
Schwartz, Marc F.
Johnson, Karl
Bowe, Caryn
Wakarchuk, Warren W.
DeFrees, Shawn
Withers, Stephen G.
Strynadka, Natalie C. J.
Source :
Nature Structural & Molecular Biology; Nov2009, Vol. 16 Issue 11, p1186-1188, 3p, 2 Diagrams
Publication Year :
2009

Abstract

Sialic acid is the most abundant terminal monosaccharide on mammalian cell surface glycoconjugates. The crystal structures of a mammalian sialyltransferase, that of porcine ST3Gal-I, in the apo form and bound to analogues of the donor and acceptor substrate are now described, providing insights into the catalytic mechanism and for inhibitor design. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
15459993
Volume :
16
Issue :
11
Database :
Complementary Index
Journal :
Nature Structural & Molecular Biology
Publication Type :
Academic Journal
Accession number :
44966283
Full Text :
https://doi.org/10.1038/nsmb.1685