Structural insight into mammalian sialyltransferases.
Mammalian cell surfaces are modified by complex arrays of glycoproteins, glycolipids and polysaccharides, many of which terminate in sialic acid and have central roles in essential processes including cell recognition, adhesion and immunogenicity. Sialylation of glycoconjugates is performed by a set of sequence-related enzymes known as sialyltransferases (STs). Here we present the crystal structure of a mammalian ST, porcine ST3Gal-I, providing a structural basis for understanding the mechanism and specificity of these enzymes and for the design of selective inhibitors.
Rao
Francesco V
FV
Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.
Rich
Jamie R
JR
Rakić
Bojana
B
Buddai
Sai
S
Schwartz
Marc F
MF
Johnson
Karl
K
Bowe
Caryn
C
Wakarchuk
Warren W
WW
Defrees
Shawn
S
Withers
Stephen G
SG
Strynadka
Natalie C J
NC
D000818:Animals; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D017433:Protein Structure, Secondary; D012799:Sialyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase