
Preliminary crystallographic analysis of the N‐terminal PDZ‐like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies
Author(s) -
Han Huijong,
Kursula Petri
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113016266
Subject(s) - pdz domain , crystallography , peripheral nervous system , gene isoform , myelin , peripheral , peripheral nerve , nervous system , biophysics , biology , chemistry , anatomy , central nervous system , microbiology and biotechnology , biochemistry , neuroscience , medicine , gene
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 P 3 1 21 or P 3 2 21, 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.