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dc.contributor.authorHan, Huijong
dc.contributor.authorKursula, Petri
dc.date.accessioned2014-05-02T14:10:50Zen
dc.date.available2014-05-02T14:10:50Zen
dc.date.issued2013-07en
dc.identifier.citationPreliminary 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.issn1744-3091en
dc.identifier.pmid23832213en
dc.identifier.doi10.1107/S1744309113016266en
dc.identifier.urihttp://hdl.handle.net/10033/316457en
dc.description.abstractPeriaxin (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.isoenen
dc.rightsArchived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communicationsen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshCrystallizationen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshHumansen
dc.subject.meshMembrane Proteinsen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshPDZ Domainsen
dc.subject.meshPeripheral Nervesen
dc.subject.meshPeripheral Nervous System Diseasesen
dc.subject.meshRecombinant Proteinsen
dc.subject.meshSequence Homology, Amino Aciden
dc.subject.meshSynchrotronsen
dc.titlePreliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies.en
dc.typeArticleen
dc.identifier.journalActa crystallographica. Section F, Structural biology and crystallization communicationsen
refterms.dateFOA2018-06-13T07:23:18Z
html.description.abstractPeriaxin (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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