Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies.
| dc.contributor.author | Han, Huijong | |
| dc.contributor.author | Kursula, Petri | |
| dc.date.accessioned | 2014-05-02T14:10:50Z | en |
| dc.date.available | 2014-05-02T14:10:50Z | en |
| dc.date.issued | 2013-07 | en |
| dc.identifier.citation | Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies. 2013, 69 (Pt 7):804-8 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. | en |
| dc.identifier.issn | 1744-3091 | en |
| dc.identifier.pmid | 23832213 | en |
| dc.identifier.doi | 10.1107/S1744309113016266 | en |
| dc.identifier.uri | http://hdl.handle.net/10033/316457 | en |
| dc.description.abstract | Periaxin (PRX) is an abundant protein in peripheral nerves and contains a predicted PDZ-like domain at its N-terminus. The large isoform, L-PRX, is required for the maintenance of myelin in the peripheral nervous system and its defects cause neurological disease. Here, the human periaxin PDZ-like domain was crystallized and X-ray diffraction data were collected to 2.85 Å resolution using synchrotron radiation. The crystal belonged to the primitive hexagonal space group P3121 or P3221, with unit-cell parameters a = b = 80.6, c = 81.0 Å, γ = 120° and either two or three molecules in the asymmetric unit. The structure of PRX will shed light on its poorly characterized function in the nervous system. | |
| dc.language.iso | en | en |
| dc.rights | Archived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communications | en |
| dc.subject.mesh | Amino Acid Sequence | en |
| dc.subject.mesh | Crystallization | en |
| dc.subject.mesh | Crystallography, X-Ray | en |
| dc.subject.mesh | Humans | en |
| dc.subject.mesh | Membrane Proteins | en |
| dc.subject.mesh | Molecular Sequence Data | en |
| dc.subject.mesh | PDZ Domains | en |
| dc.subject.mesh | Peripheral Nerves | en |
| dc.subject.mesh | Peripheral Nervous System Diseases | en |
| dc.subject.mesh | Recombinant Proteins | en |
| dc.subject.mesh | Sequence Homology, Amino Acid | en |
| dc.subject.mesh | Synchrotrons | en |
| dc.title | Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies. | en |
| dc.type | Article | en |
| dc.identifier.journal | Acta crystallographica. Section F, Structural biology and crystallization communications | en |
| refterms.dateFOA | 2018-06-13T07:23:18Z | |
| html.description.abstract | Periaxin (PRX) is an abundant protein in peripheral nerves and contains a predicted PDZ-like domain at its N-terminus. The large isoform, L-PRX, is required for the maintenance of myelin in the peripheral nervous system and its defects cause neurological disease. Here, the human periaxin PDZ-like domain was crystallized and X-ray diffraction data were collected to 2.85 Å resolution using synchrotron radiation. The crystal belonged to the primitive hexagonal space group P3121 or P3221, with unit-cell parameters a = b = 80.6, c = 81.0 Å, γ = 120° and either two or three molecules in the asymmetric unit. The structure of PRX will shed light on its poorly characterized function in the nervous system. |
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publications of the research group CSSB [12]
structural biology of the cytoskeleton

