Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide

Radu Ion Huculeci; Lieven Buts; Tom Lenaerts; Nico Van Nuland; Abel Garcia Pino

Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide

Radu Ion Huculeci, Lieven Buts, Tom Lenaerts, Nico Van Nuland, Abel Garcia Pino

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

SH2 domains are widespread protein-binding modules that recognize phosphotyrosines and play central roles in intracellular signalling pathways. The SH2 domain of the human protein tyrosine kinase Fyn has been expressed, purified and crystallized in the unbound state and in complex with a high-affinity phosphotyrosine peptide. X-ray data were collected to a resolution of 2.00 Å for the unbound form and 1.40 Å for the protein in complex with the phosphotyrosine peptide.

Original language	English
Pages (from-to)	359-364
Number of pages	6
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Publication status	Published - 1 Mar 2012

Keywords

Sh2 domains
crystallographie

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http://dx.doi.org/10.1107/S1744309112004186

Cite this

Huculeci, R. I., Buts, L., Lenaerts, T., Van Nuland, N., & Garcia Pino, A. (2012). Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68, 359-364. http://dx.doi.org/10.1107/S1744309112004186

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title = "Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide",

abstract = "SH2 domains are widespread protein-binding modules that recognize phosphotyrosines and play central roles in intracellular signalling pathways. The SH2 domain of the human protein tyrosine kinase Fyn has been expressed, purified and crystallized in the unbound state and in complex with a high-affinity phosphotyrosine peptide. X-ray data were collected to a resolution of 2.00 {\AA} for the unbound form and 1.40 {\AA} for the protein in complex with the phosphotyrosine peptide.",

keywords = "Sh2 domains, crystallographie",

author = "Huculeci, {Radu Ion} and Lieven Buts and Tom Lenaerts and {Van Nuland}, Nico and {Garcia Pino}, Abel",

year = "2012",

month = mar,

day = "1",

language = "English",

volume = "68",

pages = "359--364",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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Huculeci, RI, Buts, L , Lenaerts, T, Van Nuland, N & Garcia Pino, A 2012, 'Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 68, pp. 359-364. <http://dx.doi.org/10.1107/S1744309112004186>

Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide. / Huculeci, Radu Ion; Buts, Lieven ; Lenaerts, Tom et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 68, 01.03.2012, p. 359-364.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide

AU - Huculeci, Radu Ion

AU - Buts, Lieven

AU - Lenaerts, Tom

AU - Van Nuland, Nico

AU - Garcia Pino, Abel

PY - 2012/3/1

Y1 - 2012/3/1

N2 - SH2 domains are widespread protein-binding modules that recognize phosphotyrosines and play central roles in intracellular signalling pathways. The SH2 domain of the human protein tyrosine kinase Fyn has been expressed, purified and crystallized in the unbound state and in complex with a high-affinity phosphotyrosine peptide. X-ray data were collected to a resolution of 2.00 Å for the unbound form and 1.40 Å for the protein in complex with the phosphotyrosine peptide.

AB - SH2 domains are widespread protein-binding modules that recognize phosphotyrosines and play central roles in intracellular signalling pathways. The SH2 domain of the human protein tyrosine kinase Fyn has been expressed, purified and crystallized in the unbound state and in complex with a high-affinity phosphotyrosine peptide. X-ray data were collected to a resolution of 2.00 Å for the unbound form and 1.40 Å for the protein in complex with the phosphotyrosine peptide.

KW - Sh2 domains

KW - crystallographie

M3 - Article

SN - 1744-3091

VL - 68

SP - 359

EP - 364

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ER -

Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide

Abstract

Keywords

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