Dimerization effect of sucrose octasulfate on rat FGF1.

Research output: Contribution to journalJournal articlepeer-review

Standard

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 articlepeer-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., Bock, E. M., & 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