Dimerization effect of sucrose octasulfate on rat FGF1.

Research output: Contribution to journalJournal articleResearchpeer-review

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Dimerization effect of sucrose octasulfate on rat FGF1. / Kulahin, Nikolaj; Kiselyov, Vladislav; Kochoyan, Artur; Kristensen, Ole; Kastrup, Jette Sandholm Jensen; Berezin, Vladimir; Bock, Elisabeth Marianne; Gajhede, Michael.

In: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Vol. 64, No. Pt6, 2008, p. 448-452.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Kulahin, N, Kiselyov, V, Kochoyan, A, Kristensen, O, Kastrup, JSJ, Berezin, V, Bock, EM & Gajhede, M 2008, 'Dimerization effect of sucrose octasulfate on rat FGF1.', Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, vol. 64, no. Pt6, pp. 448-452. https://doi.org/10.1107/S174430910801066X

APA

Kulahin, N., Kiselyov, V., Kochoyan, A., Kristensen, O., Kastrup, J. S. J., Berezin, V., ... Gajhede, M. (2008). Dimerization effect of sucrose octasulfate on rat FGF1. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, 64(Pt6), 448-452. https://doi.org/10.1107/S174430910801066X

Vancouver

Kulahin N, Kiselyov V, Kochoyan A, Kristensen O, Kastrup JSJ, Berezin V et al. Dimerization effect of sucrose octasulfate on rat FGF1. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2008;64(Pt6):448-452. https://doi.org/10.1107/S174430910801066X

Author

Kulahin, Nikolaj ; Kiselyov, Vladislav ; Kochoyan, Artur ; Kristensen, Ole ; Kastrup, Jette Sandholm Jensen ; Berezin, Vladimir ; Bock, Elisabeth Marianne ; Gajhede, Michael. / Dimerization effect of sucrose octasulfate on rat FGF1. In: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2008 ; Vol. 64, No. Pt6. pp. 448-452.

Bibtex

@article{b0e652e0eb9211ddbf70000ea68e967b,
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",
note = "Paper id:: 18540049",
year = "2008",
doi = "10.1107/S174430910801066X",
language = "English",
volume = "64",
pages = "448--452",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt6",

}

RIS

TY - JOUR

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

VL - 64

SP - 448

EP - 452

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt6

ER -

ID: 9936088