4o6x | pdb_00004o6x

Crystal structure of human Ankyrin G death domain

spinqualitylabelsall models 4o6x, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4o6x 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. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease ANK3_HUMAN Intellectual disability - hypotonia - spasticity - sleep disorder;Schizophrenia. Genetic variations in ANK3 may be associated with autism spectrum disorders susceptibility. The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in ANK3 predicted to result in frameshift and premature truncation, has been shown to be the cause of moderate intellectual disability, an ADHD-like phenotype and behavioral problems in a consanguineous family (PubMed:23390136). Function ANK3_HUMAN In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. Isoform 5: May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin. Publication Abstract from PubMed Ankyrins (Ank) are a ubiquitously expressed family of multifunctional membrane adapter proteins. Ankyrin G (AnkG) is critical for assembling and maintenance of the axon initial segment. Here we present the 2.1 A crystal structure of human AnkG death domain (hAnkG-DD). The core death domain is composed of six alpha-helices and three 310 -helices. It forms a hydrophobic pocket on the surface of the molecule. The C-terminal tail of the hAnkG-DD curves back to have the aromatic ring of a phenylalanine residue, Phe100 insert into this pocket, which anchors the flexible tail onto the core domain. Related DDs were selected for structure comparison. The major variations are at the C-terminal region, including the alpha6 and the long C-terminal extension. The results of size exclusion chromatography and analytical ultracentrifugation suggest that hAnkG-DD exists as monomer in solution. Our work should help for the future investigation of the structure-function of AnkG.Proteins 2014. (c) 2014 Wiley Periodicals, Inc. Crystal structure of human Ankyrin G death domain.,Liu Y, Zhang Y, Wang JH Proteins. 2014 Oct 11. doi: 10.1002/prot.24702. PMID:25307106 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ankyrin 3D structures

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