Dimerization effect of sucrose octasulfate on rat FGF1.

Nikolaj Kulahin; Vladislav Kiselyov; Artur Kochoyan; Ole Kristensen; Jette Sandholm Jensen Kastrup; Vladimir Berezin; Elisabeth Marianne Bock; Michael Gajhede

doi:10.1107/S174430910801066X

Dimerization effect of sucrose octasulfate on rat FGF1.

Nikolaj Kulahin, Vladislav Kiselyov, Artur Kochoyan, Ole Kristensen, Jette Sandholm Jensen Kastrup, Vladimir Berezin, Elisabeth Marianne Bock, Michael Gajhede

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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.

Original language	English
Journal	Acta Crystallographica. Section F : Structural Biology and Crystallization Communications
Volume	64
Issue number	Pt6
Pages (from-to)	448-452
Number of pages	5
ISSN	1744-3091
DOIs	https://doi.org/10.1107/S174430910801066X
Publication status	Published - 2008

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title = "Dimerization effect of sucrose octasulfate on rat FGF1.",

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.",

author = "Nikolaj Kulahin and Vladislav Kiselyov and Artur Kochoyan and Ole Kristensen and Kastrup, {Jette Sandholm Jensen} and Vladimir Berezin and Bock, {Elisabeth Marianne} and Michael Gajhede",

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T1 - Dimerization effect of sucrose octasulfate on rat FGF1.

AU - Kulahin, Nikolaj

AU - Kiselyov, Vladislav

AU - Kochoyan, Artur

AU - Kristensen, Ole

AU - Kastrup, Jette Sandholm Jensen

AU - Berezin, Vladimir

AU - Bock, Elisabeth Marianne

AU - Gajhede, Michael

N1 - Paper id:: 18540049

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1107/S174430910801066X

DO - 10.1107/S174430910801066X

M3 - Journal article

C2 - 18540049

SN - 2053-230X

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JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Pt6

ER -

Dimerization effect of sucrose octasulfate on rat FGF1.

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