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.
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.
Kochoyan
Artur
A
The Protein Laboratory, Department of Neuroscience and Pharmacology, Faculty of Health Sciences, Panum Institute, University of Copenhagen, Blegdamsvej 3C, Building 24.2, 2200 Copenhagen N, Denmark. arturkochoyan@gmail.com
Poulsen
Flemming M
FM
Berezin
Vladimir
V
Bock
Elisabeth
E
Kiselyov
Vladislav V
VV
D000595:Amino Acid Sequence; D000818:Animals; D003461:Crystallography; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry*; D007136:Immunoglobulins / Q000737:chemistry*; D051379:Mice; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D051496:Receptor, Fibroblast Growth Factor, Type 1 / Q000737:chemistry*; D020349:Surface Plasmon Resonance
D007136:Immunoglobulins; D016220:Fibroblast Growth Factor 1; C496349:Fgfr1 protein, mouse; D051496:Receptor, Fibroblast Growth Factor, Type 1