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BibTeX file of [Han14] [show it without abstract]

@article{Han14, author={Huijong Han and Petri Kursula}, title={Periaxin and {AHNAK} nucleoprotein 2 form intertwined homodimers through domain swapping}, journal={J. Biol. Chem.}, volume={289}, pages={14121--14131}, year={2014}, url={https://doi.org/10.1074/jbc.M114.554816}, doi={10.1074/jbc.M114.554816}, abstract={Periaxin (PRX) is an abundant protein in the peripheral nervous system, with an important role in myelination. PRX participates in large molecular complexes, most likely through the interactions of its N-terminal PSD-95/Discs-large/ZO-1 (PDZ)-like domain. We present the crystal structures of the PDZ-like domains from PRX and its homologue AHNAK nucleoprotein 2 (AHNAK2). The unique intertwined, domain-swapped dimers provide a structural basis for the homodimerization of both proteins. The core of the homodimer is formed by a 6-stranded antiparallel $\beta$ sheet, with every other strand from a different chain. The AHNAK2 PDZ domain structure contains a bound class III ligand peptide. The binding pocket is preformed, and the peptide-PDZ interactions have unique aspects, including two salt bridges and weak recognition of the peptide C terminus. Tight homodimerization may be central to the scaffolding functions of PRX and AHNAK2 in molecular complexes linking the extracellular matrix to the cytoskeletal network.} }

Huijong Han and Petri Kursula, Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping, J. Biol. Chem. 289, 14121–14131 (2014)

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[abstract]

doi:10.1074/jbc.M114.554816

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