Ankyrin
From Proteopedia
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| - | < | + | <StructureSection load='1n11' size='350' side='right' scene='45/454440/Cv/1' caption='Human ankyrin-1 ankyrin repeat region (containing 12 repeats) complex with Cl- (green) and Br- (dark red) ions [[1n11]]'> |
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== Function == | == Function == | ||
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In mammals ANK is encoded by 3 genes: ANK1, ANK2 and ANK3.<br /> | In mammals ANK is encoded by 3 genes: ANK1, ANK2 and ANK3.<br /> | ||
| - | *'''ANK1''' or '''ankyrin-R'''is found in erythrocytes, brain and muscle.<br /> | + | *'''ANK1''' or '''ankyrin-R''' is found in erythrocytes, brain and muscle.<br /> |
*'''ANK2''' or '''ankyrin-B''' is found in brain and muscle.<br /> | *'''ANK2''' or '''ankyrin-B''' is found in brain and muscle.<br /> | ||
*'''ANK3''' or '''ankyrin-G''' is found in the nervous system and associates with Na channels.<br /> | *'''ANK3''' or '''ankyrin-G''' is found in the nervous system and associates with Na channels.<br /> | ||
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| + | '''Gankyrin''' or '''26S proteasome non-ATPase regulatory subunit 10''' (GANK) is an oncoprotein which is a component of the 19S cap of the proteasome. GANK contains ankyrin repeats. | ||
== Disease == | == Disease == | ||
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Mutations in erythrocyte ANK1 are associated with spherocytosis. Mutations in ANK2 are associated with cardiac arrhythmia syndrome. Mutations in ANK3 are associated with bipolar disorder. | Mutations in erythrocyte ANK1 are associated with spherocytosis. Mutations in ANK2 are associated with cardiac arrhythmia syndrome. Mutations in ANK3 are associated with bipolar disorder. | ||
| - | == | + | == Relevance == |
| - | + | GANK is overexpressed in hepatocellular carcinoma. | |
| - | == | + | == Structural highlights == |
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| - | + | Ankyrin contains four domains: the N terminal which contains 24 ankyrin repeats, a spectrin-binding domain, a death domain which binds to proteins involved in apoptosis and a C terminal regulatory domain. The full-length 328-amino acid mouse protein contains an ATP/GTP-binding domain in its N-terminal half and an ankyrin repeat region in its C-terminal half. It also has a nuclear localization signal, 2 protein-destabilizing PEST sequences, and 2 phosphorylation sites. The '''ankyrin repeat''' is a protein-protein interaction motif. It is a 33 residue segment consisting of a helix-loop-helix motif. The long ankyrin repeat in human ankyrin-R contains 12 ankyrin repeats (residues 402-827) and is called D34 region. <scene name='45/454440/Cv/2'>Click here to see 12 ankyrin repeats</scene>. <ref>PMID:12456646</ref> <scene name='45/454440/Cv/3'>One ankyrin repeat</scene> from [[1n0r]]. <ref>PMID:12461176</ref> | |
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| - | + | == 3D Structures of ankyrin == | |
| + | [[Ankyrin 3D structures]] | ||
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| + | </StructureSection> | ||
| - | + | == References == | |
| - | + | <references/> | |
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
- ↑ Mosavi LK, Minor DL Jr, Peng ZY. Consensus-derived structural determinants of the ankyrin repeat motif. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16029-34. Epub 2002 Dec 2. PMID:12461176 doi:http://dx.doi.org/10.1073/pnas.252537899
