2UUS

Crystal structure of the rat FGF1-sucrose octasulfate (SOS) complex.

Summary for 2UUS

• Entry DOI: 10.2210/pdb2uus/pdb
• Related: 2J3P
• Related PRD ID: PRD_900013
• Descriptor: HEPARIN-BINDING GROWTH FACTOR 1, 1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose-(2-1)-2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: differentiation, heparin-binding, sucrose octasulfate, developmental protein, fibroblast growth factor, mitogen, angiogenesis, growth factor
• Biological source: RATTUS NORVEGICUS (RAT)
• Total number of polymer chains: 2
• Total formula weight: 30930.55

Authors

Kulahin, N.,Kiselyov, V.,Kochoyan, A.,Kristensen, O.,Berezin, V.,Bock, E.,Gajhede, M. (deposition date: 2007-03-07, release date: 2008-05-13, Last modification date: 2023-12-13)

Primary citation

Kulahin, N.,Kiselyov, V.,Kochoyan, A.,Kristensen, O.,Kastrup, J.S.,Berezin, V.,Bock, E.,Gajhede, M.
Dimerization Effect of Sucrose Octasulfate on Rat Fgf1.
Acta Crystallogr.,Sect.F, 64:448-, 2008

PubMed 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.

PubMed: 18540049
DOI: 10.1107/S174430910801066X

Experimental method

X-RAY DIFFRACTION (2.2 Å)