Structural observation of complexes of FGF-2 and regioselectively desulfated heparin in aqueous solutions.
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.
Yuguchi
Yoshiaki
Y
National Institute of Advanced and Industrial Science and Technology, 2266-98 Anagahora, Shimo-shidanmi, Moriyama-ku, Nagoya, Aichi 463-8560, Japan. y-yuguchi@aist.go.jp
Kominato
Rieko
R
Ban
Tadato
T
Urakawa
Hiroshi
H
Kajiwara
Kanji
K
Takano
Ryo
R
Kamei
Kaeko
K
Hara
Saburo
S
D002236:Carbohydrate Conformation; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry*; D006493:Heparin / Q000737:chemistry*; D006801:Humans; D007067:Iduronic Acid / Q000737:chemistry; D008956:Models, Chemical; D015233:Models, Statistical; D008968:Molecular Conformation; D012542:Scattering, Radiation; D015398:Signal Transduction; D013431:Sulfates / Q000737:chemistry; D013455:Sulfur / Q000737:chemistry; D014867:Water / Q000737:chemistry; D014965:X-Rays
D013431:Sulfates; D014867:Water; D016222:Fibroblast Growth Factor 2; D007067:Iduronic Acid; D013455:Sulfur; D006493:Heparin