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PDBsum entry 2uus

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Growth factor PDB id
2uus
Contents
Protein chains
132 a.a.
Ligands
GU4-YYJ
Waters ×163

References listed in PDB file
Key reference
Title Dimerization effect of sucrose octasulfate on rat fgf1.
Authors N.Kulahin, V.Kiselyov, A.Kochoyan, O.Kristensen, J.S.Kastrup, V.Berezin, E.Bock, M.Gajhede.
Ref. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008, 64, 448-452.
PubMed id 18540049
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 A 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.
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