An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope

P. D. Carr; F. Conlan; S. Ford; D. L. Ollis; I. G. Young

doi:10.1107/S1744309106016812

An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope

P. D. Carr^*
, F. Conlan
, S. Ford
, D. L. Ollis
, I. G. Young

^*Corresponding author for this work

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

26 Citations (Scopus)

Abstract

X-ray diffraction has been used to produce and refine a model of the extracellular domains of the β common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.

Original language	English
Pages (from-to)	509-513
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	6
DOIs	https://doi.org/10.1107/S1744309106016812
Publication status	Published - Jun 2006

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Carr, P. D., Conlan, F., Ford, S., Ollis, D. L., & Young, I. G. (2006). An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(6), 509-513. https://doi.org/10.1107/S1744309106016812

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title = "An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope",

abstract = "X-ray diffraction has been used to produce and refine a model of the extracellular domains of the β common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.",

author = "Carr, \{P. D.\} and F. Conlan and S. Ford and Ollis, \{D. L.\} and Young, \{I. G.\}",

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language = "English",

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pages = "509--513",

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Carr, PD, Conlan, F, Ford, S, Ollis, DL & Young, IG 2006, 'An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 6, pp. 509-513. https://doi.org/10.1107/S1744309106016812

An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope. / Carr, P. D.; Conlan, F.; Ford, S. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 6, 06.2006, p. 509-513.

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

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AU - Ollis, D. L.

AU - Young, I. G.

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AB - X-ray diffraction has been used to produce and refine a model of the extracellular domains of the β common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.

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An improved resolution structure of the human β common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope

Abstract

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