2uus
From Proteopedia
CRYSTAL STRUCTURE OF THE RAT FGF1-SUCROSE OCTASULFATE (SOS) COMPLEX.
Overview
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.
About this Structure
2UUS is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Dimerization effect of sucrose octasulfate on rat FGF1., Kulahin N, Kiselyov V, Kochoyan A, Kristensen O, Kastrup JS, Berezin V, Bock E, Gajhede M, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):448-52. Epub 2008 May 16. PMID:18540049 Page seeded by OCA on Wed Jun 18 12:17:34 2008
