Abstract
Fibroblast growth factors (FGFs) constitute a family of at least 23 structurally related heparin-binding proteins that are involved in regulation of cell growth, survival, differentiation and migration. Sucrose octasulfate (SOS), a chemical analogue of heparin, has been demonstrated to activate FGF signalling pathways. The structure of rat FGF1 crystallized in the presence of SOS has been determined at 2.2 Å resolution. SOS-mediated dimerization of FGF1 was observed, which was further supported by gel-filtration experiments. The major contributors to the sulfate-binding sites in rat FGF1 are Lys113, Lys118, Arg122 and Lys128. An arginine at position 116 is a consensus residue in mammalian FGF molecules; however, it is a serine in rat FGF1. This difference may be important for SOS-mediated FGF1 dimerization in rat. © 2008 International Union of Crystallography All rights reserved.
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Kulahin, N., Kiselyov, V., Kochoyan, A., Kristensen, O., Kastrup, J. S., Berezin, V., … Gajhede, M. (2008). Dimerization effect of sucrose octasulfate on rat FGF1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(6), 448–452. https://doi.org/10.1107/S174430910801066X
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