4cn0

An intertwined homodimer of the PDZ homology domain of AHNAK2

spinqualitylabelsall models 4cn0, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cn0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: K, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AHNK2_HUMAN Publication Abstract from PubMed 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. Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping.,Han H, Kursula P J Biol Chem. 2014 Mar 27. PMID:24675079 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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