A triple-binding-domain model explains the specificity of the interaction of a sphingolipid activator protein (SAP-1) with sulphatide, GM1-ganglioside and globotriaosylceramide
Keyword(s):
The conformations of the neutral glycosphingolipid, globotriaosylceramide, and of the methyl ester of GM1-ganglioside have been predicted by energy-minimization techniques and compared with those previously obtained for GM1- and GM2-ganglioside. A triple-binding-domain model is put forward to explain known specificities of binding between these glycosphingolipids and activator proteins. This model suggests that hydrophobic interactions, electrostatic interactions and hydrogen-bonding between sugar residues are important. The model is discussed in relation to previous studies on the effect of chemical modification of glycosphingolipids on their ligand properties.
1997 ◽
Vol 38
(11)
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pp. 1933-1936
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1990 ◽
Vol 10
(10)
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pp. 5128-5137
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2001 ◽
Vol 13
(5)
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pp. 619-625
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2004 ◽
Vol 60
(1)
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pp. 90-96
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2002 ◽
Vol 68
(8)
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pp. 3965-3968
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