Fujii, Kotaro, Young, Mark Thomas  ORCID: https://orcid.org/0000-0002-9615-9002 and Harris, Kenneth David Maclean ORCID: https://orcid.org/0000-0001-7855-8598
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: | Professional Services > Advanced Research Computing @ Cardiff (ARCCA) Schools > Chemistry Schools > 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: | 24 May 2023 16:57 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/12058 |
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