Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods

被引：18

作者：

Canales-Mayordomo, Angeles

Fayos, Rosa

Angulo, Jesus

Ojeda, Rafael

Martin-Pastor, Manuel

Nieto, Pedro M.

Martin-Lomas, Manuel

Lozano, Rosa

Gimenez-Gallego, Guillermo

Jimenez-Barbero, Jesus

机构：

[1] CSIC, Ctr Invest Biol, Dept Estruct & Func Prot, E-28006 Madrid, Spain

[2] CSIC, Inst Invest Quim, Grp Carbohidratos, Seville 41092, Spain

[3] CSIC, Lab Estruct & Estruct Biomol Jose Carracido, Unidad RM, Santiago De Compostela, Spain

[4] CSIC, Lab Estruct & Estruct Biomol Jose Carracido, Unidad RMN Biomol Asoc, Santiago De Compostela, Spain

来源：

JOURNAL OF BIOMOLECULAR NMR | 2006年 / 35卷 / 04期

关键词：

chemical shift perturbation; fibroblast growth factors; heparan sulfate oligosaccharides; protein-carbohydrate interactions; relaxation analysis;

D O I：

10.1007/s10858-006-9024-y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The binding site and backbone dynamics of a bioactive complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed heparin hexasaccharide has been investigated by HSQC and relaxation NMR methods. The comparison of the relaxation data for the free and bound states has allowed showing that the complex is monomeric, and still induces mutagenesis, and that the protein backbone presents reduced motion in different timescale in its bound state, except in certain points that are involved in the interaction with the fibroblast growth factor receptor (FGFR).

引用

页码：225 / 239

页数：15

共 68 条

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