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Exploiting powder X-ray diffraction for direct structure determination in structural biology: the P2X4 receptor trafficking motif YEQGL

Fujii, Kotaro, Young, Mark Thomas and Harris, Kenneth David Maclean 2011. Exploiting powder X-ray diffraction for direct structure determination in structural biology: the P2X4 receptor trafficking motif YEQGL. Journal of Structural Biology 174 (3) , pp. 461-467. 10.1016/j.jsb.2011.03.001

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Abstract

We report the crystal structure of the 5-residue peptide acetyl-YEQGL-amide, determined directly from powder X-ray diffraction data recorded on a conventional laboratory X-ray powder diffractometer. The YEQGL motif has a known biological role, as a trafficking motif in the C-terminus of mammalian P2X4 receptors. Comparison of the crystal structure of acetyl-YEQGL-amide determined here and that of a complex formed with the μ2 subunit of the clathrin adaptor protein complex AP2 reported previously, reveals differences in conformational properties, although there are nevertheless similarities concerning aspects of the hydrogen-bonding arrangement and the hydrophobic environment of the leucine sidechain. Our results demonstrate the potential for exploiting modern powder X-ray diffraction methodology to achieve complete structure determination of materials of biological interest that do not crystallize as single crystals of suitable size and quality for single-crystal X-ray diffraction.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Advanced Research Computing @ Cardiff (ARCCA)
Chemistry
Biosciences
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Uncontrolled Keywords: P2X ; Powder X-ray diffraction ; Trafficking ; Direct-space structure solution ; Genetic algorithm Structure determination
Publisher: Elsevier
ISSN: 1047-8477
Date of First Compliant Deposit: 30 March 2016
Last Modified: 02 May 2019 12:11
URI: http://orca.cf.ac.uk/id/eprint/12058

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