4CMZ
An intertwined homodimer of the PDZ homology domain of periaxin
Summary for 4CMZ
| Entry DOI | 10.2210/pdb4cmz/pdb |
| Descriptor | PERIAXIN (2 entities in total) |
| Functional Keywords | cell cycle, domain swapping, intertwining |
| Biological source | Homo sapiens (HUMAN) |
| Cellular location | Isoform 1: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Isoform 2: Cytoplasm . Cell membrane : Q9BXM0 |
| Total number of polymer chains | 3 |
| Total formula weight | 30135.88 |
| Authors | Han, H.,Kursula, P. (deposition date: 2014-01-20, release date: 2014-04-02, Last modification date: 2024-05-08) |
| Primary citation | Han, H.,Kursula, P. Periaxin and Ahnak Nucleoprotein 2 Form Intertwined Homodimers Through Domain Swapping J.Biol.Chem., 289:14121-, 2014 Cited by PubMed 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 β 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. PubMed: 24675079DOI: 10.1074/JBC.M114.554816 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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