Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9890942 | International Journal of Biological Macromolecules | 2005 | 7 Pages |
Abstract
In order to clarify the mechanism of interaction between FGF-2 and heparin, the association structures between human FGF-2 and different kinds of regioselectively desulfated heparins were observed by small angle X-ray scattering. In the FGF-2-native heparin complex, the global FGF-2 molecules appeared to attach along heparin chain as strained unilaterally. The complexes with the 6-O-, or N-desulfated heparin seemed to have randomly associated structure as compared with above system. On the other hand, 2-O-desulfated heparin did not indicate the aggregation with FGF-2, indicating that the sulfate groups at O-2 of iduronate residues in heparin is most essential for association with FGF-2. These structural characteristics will be deeply related with signal transduction in the association with FGF-2 receptor.
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Authors
Yoshiaki Yuguchi, Rieko Kominato, Tadato Ban, Hiroshi Urakawa, Kanji Kajiwara, Ryo Takano, Kaeko Kamei, Saburo Hara,