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4o6x

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'''Unreleased structure'''
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==Crystal structure of human Ankyrin G death domain==
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<StructureSection load='4o6x' size='340' side='right' caption='[[4o6x]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4o6x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O6X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O6X FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3psp|3psp]], [[3pst|3pst]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o6x RCSB], [http://www.ebi.ac.uk/pdbsum/4o6x PDBsum]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/ANK3_HUMAN 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).<ref>PMID:23390136</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/ANK3_HUMAN 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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4o6x is ON HOLD until Paper Publication
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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<ref>PMID:25307106</ref>
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Authors: Liu, Y., Zhang, Y., Wang, J.H.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of human Ankyrin G death domain
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Liu, Y.]]
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[[Category: Wang, J H.]]
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[[Category: Zhang, Y.]]
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[[Category: Alpha helix]]
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[[Category: Alpha helix bundle]]
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[[Category: Death domain]]
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[[Category: Protein binding]]

Revision as of 11:13, 29 October 2014

Crystal structure of human Ankyrin G death domain

4o6x, resolution 2.10Å

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