Ankyrin
From Wikipedia, the free encyclopedia
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| Ribbon diagram of a fragment of the membrane-binding domain of ankyrin 1. From PDB 1N11. | |
| Identifiers | |
| Symbol | ANK1 |
| Alt. Symbols | ANK |
| Entrez | 286 |
| HUGO | 492 |
| OMIM | 182900 |
| RefSeq | NM_000037 |
| UniProt | P16157 |
| Other data | |
| Locus | Chr. 8 p21.1-11.2 |
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ankyrin 2, neuronal
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| Identifiers | |
| Symbol | ANK2 |
| Alt. Symbols | LQT4 |
| Entrez | 287 |
| HUGO | 493 |
| OMIM | 106410 |
| RefSeq | NM_001148 |
| UniProt | Q01484 |
| Other data | |
| Locus | Chr. 4 q25-q27 |
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ankyrin 3, node of Ranvier (ankyrin G)
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| Identifiers | |
| Symbol | ANK3 |
| Entrez | 288 |
| HUGO | 494 |
| OMIM | 600465 |
| RefSeq | NM_020987 |
| UniProt | Q12955 |
| Other data | |
| Locus | Chr. 10 q21 |
Ankyrins are a family of proteins that mediates the attachment of integral membrane proteins to the cytoskeleton.[1]
Ankyrin 1, was first discovered in the erythrocytes but also later found to be expressed in the brain and muscles. In erythrocytes, Ankyrin 1 links membrane receptor CD44 to inositol triphosphate and the cytoskeleton.[2]
Ankyrin contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD) consisting of 22–24 tandem repeats of 33 amino acids, a spectrin binding domain and a variably sized C-terminal regulatory domain. A single ankyrin repeat consists of a beta strand followed by two alpha helices and then another beta strand. The beta strands on adjacent ankyrin repeats combine to form a short antiparallel beta sheet.
Ankyrin was discovered by Dr. G. Vann Bennett (M.D., PhD.) in 1979.[3]
[edit] References
- ^ Hryniewicz-Jankowska A, Czogalla A, Bok E, Sikorsk AF (2002). "Ankyrins, multifunctional proteins involved in many cellular pathways". Folia Histochem Cytobiol 40 (3): 239–49. PMID 12219834.
- ^ Singleton PA, Bourguignon LY (2004). "CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation". Exp Cell Res 295 (1): 102–18. doi:. PMID 15051494.
- ^ Bennett V, Stenbuck PJ (1979). "Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin". J Biol Chem 254 (7): 2533–41. PMID 372182.
