These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A triple-binding-domain model explains the specificity of the interaction of a sphingolipid activator protein (SAP-1) with sulphatide, GM1-ganglioside and globotriaosylceramide.
    Author: Wynn CH.
    Journal: Biochem J; 1986 Dec 15; 240(3):921-4. PubMed ID: 3827882.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]