Title : The heparin binding motif of endostatin mediates its interaction with receptor nucleolin.

Pub. Date : 2009 Dec 15

PMID : 19877579






3 Functional Relationships(s)
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1 Here we show that Arg to Ala point mutagenesis of the heparin binding motif does not interrupt the folding of endostatin but significantly impairs the interaction between endostatin and nucleolin. Arginine nucleolin Homo sapiens
2 Double and quadruple mutants showed significantly decreased internalization to endothelial cells and antitumor activities, while the hexad Arg to Ala mutant completely lost its interaction with nucleolin and biological functions. Arginine nucleolin Homo sapiens
3 Taken together, the present study demonstrates that the arginine clusters in the heparin binding motif of endostatin significantly contribute to its interaction with receptor nucleolin and mediate the antiangiogenic and antitumor activities of endostatin. Arginine nucleolin Homo sapiens