Study of the interaction of the Ig2 module of the fibroblast growth factor receptor, FGFR Ig2, with the fibroblast growth factor 1, FGF1, by means of NMR spectroscopy

Artur Kochoyan; Flemming M Poulsen; Vladimir Berezin; Elisabeth Bock; Vladislav V Kiselyov

doi:10.1016/j.febslet.2008.08.033

Study of the interaction of the Ig2 module of the fibroblast growth factor receptor, FGFR Ig2, with the fibroblast growth factor 1, FGF1, by means of NMR spectroscopy

Artur Kochoyan, Flemming M Poulsen, Vladimir Berezin, Elisabeth Bock, Vladislav V Kiselyov

5 Citations (Scopus)

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Abstract

Fibroblast growth factor (FGF) receptor (FGFR) consists extracellularly of three immunoglobulin (Ig) modules (Ig1-3). Currently, there are two competing models (symmetric and asymmetric) of the FGF-FGFR-heparin complex based on crystal structures. Indirect evidence exists in support of both models. However, it is not clear which model is physiologically relevant. Our aim was to obtain direct, non-crystallographic evidence in support of them. We found by nuclear magnetic resonance that Ig2 could bind to FGF1 not only via the primary site (present in both models), but also via the secondary site (present only in the symmetric model). Thus, our data support the symmetric model.

Original language	English
Journal	FEBS Letters
Volume	582
Issue number	23-24
Pages (from-to)	3374-3378
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2008.08.033
Publication status	Published - 2008

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Study of the interaction of the Ig2 module of the fibroblast growth factor receptor, FGFR Ig2, with the fibroblast growth factor 1, FGF1, by means of NMR spectroscopy. / Kochoyan, Artur; Poulsen, Flemming M; Berezin, Vladimir et al.

In: FEBS Letters, Vol. 582, No. 23-24, 2008, p. 3374-3378.

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title = "Study of the interaction of the Ig2 module of the fibroblast growth factor receptor, FGFR Ig2, with the fibroblast growth factor 1, FGF1, by means of NMR spectroscopy",

abstract = "Fibroblast growth factor (FGF) receptor (FGFR) consists extracellularly of three immunoglobulin (Ig) modules (Ig1-3). Currently, there are two competing models (symmetric and asymmetric) of the FGF-FGFR-heparin complex based on crystal structures. Indirect evidence exists in support of both models. However, it is not clear which model is physiologically relevant. Our aim was to obtain direct, non-crystallographic evidence in support of them. We found by nuclear magnetic resonance that Ig2 could bind to FGF1 not only via the primary site (present in both models), but also via the secondary site (present only in the symmetric model). Thus, our data support the symmetric model.",

author = "Artur Kochoyan and Poulsen, {Flemming M} and Vladimir Berezin and Elisabeth Bock and Kiselyov, {Vladislav V}",

note = "Keywords: Amino Acid Sequence; Animals; Crystallography; Fibroblast Growth Factor 1; Immunoglobulins; Mice; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Interaction Mapping; Receptor, Fibroblast Growth Factor, Type 1; Surface Plasmon Resonance",

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T1 - Study of the interaction of the Ig2 module of the fibroblast growth factor receptor, FGFR Ig2, with the fibroblast growth factor 1, FGF1, by means of NMR spectroscopy

AU - Kochoyan, Artur

AU - Poulsen, Flemming M

AU - Berezin, Vladimir

AU - Bock, Elisabeth

AU - Kiselyov, Vladislav V

N1 - Keywords: Amino Acid Sequence; Animals; Crystallography; Fibroblast Growth Factor 1; Immunoglobulins; Mice; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Interaction Mapping; Receptor, Fibroblast Growth Factor, Type 1; Surface Plasmon Resonance

PY - 2008

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N2 - Fibroblast growth factor (FGF) receptor (FGFR) consists extracellularly of three immunoglobulin (Ig) modules (Ig1-3). Currently, there are two competing models (symmetric and asymmetric) of the FGF-FGFR-heparin complex based on crystal structures. Indirect evidence exists in support of both models. However, it is not clear which model is physiologically relevant. Our aim was to obtain direct, non-crystallographic evidence in support of them. We found by nuclear magnetic resonance that Ig2 could bind to FGF1 not only via the primary site (present in both models), but also via the secondary site (present only in the symmetric model). Thus, our data support the symmetric model.

AB - Fibroblast growth factor (FGF) receptor (FGFR) consists extracellularly of three immunoglobulin (Ig) modules (Ig1-3). Currently, there are two competing models (symmetric and asymmetric) of the FGF-FGFR-heparin complex based on crystal structures. Indirect evidence exists in support of both models. However, it is not clear which model is physiologically relevant. Our aim was to obtain direct, non-crystallographic evidence in support of them. We found by nuclear magnetic resonance that Ig2 could bind to FGF1 not only via the primary site (present in both models), but also via the secondary site (present only in the symmetric model). Thus, our data support the symmetric model.

U2 - 10.1016/j.febslet.2008.08.033

DO - 10.1016/j.febslet.2008.08.033

M3 - Journal article

C2 - 18786534

SN - 0014-5793

VL - 582

SP - 3374

EP - 3378

JO - F E B S Letters

JF - F E B S Letters

IS - 23-24

ER -

Study of the interaction of the Ig2 module of the fibroblast growth factor receptor, FGFR Ig2, with the fibroblast growth factor 1, FGF1, by means of NMR spectroscopy

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