Spectrin
From Proteopedia
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FunctionSpectrin forms scaffolding in plasma membranes and cytoskeletal structure. It interacts with actin at either end of its tetramer[1]. The SPT dimer is formed by association of α1 and β1 monomers. In invertebrates there are SPT α, β and βH. In vertebrates there are SPT α1 (SPTA1), α2 (SPTA2) and β1 (SPTB1) to β5. SPT contains an SRC Homology 3 domain (SH3), a Pleckstrin Homology (PH) domain and a Calponin Homology (CH) domain. DiseaseMutations in SPT α are found in patients with hereditary elliptocytosis[2]. SPT β deficiency is found in hereditary spherocytosis[3].
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3D Structures of Spectrin
Updated on 04-October-2017
{"openlevels":0}
- Spectrin α1
- Spectrin α2
- Spectrin α
- 1uue, 1e7o, 1g2b, 1aey, 1tuc, 1tud - cSPTA SH3 domain (mutant) – NMR
- 2lj3 - cSPTA SH3 domain – NMR
- 1e6g, 1e6h, 1hd3, 1qkx, 1pwt, 1bk2, 1shg - cSPTA SH3 domain (mutant)
- 1u4q – cSPTA repeats 15-17
- 1u5p - cSPTA repeats 15-16
- 1cun - cSPTA repeats 16-17
- 1aj3 - cSPTA repeat 16 - NMR
- 1owa - hSPTA tetramerization domain – NMR
- 1h8k, 3ngp, 3m0p, 3m0q, 3m0r, 3m0s, 3m0t, 3m0u – cSPTA SH3 domain (mutant)
- 2kr3, 4f17, 4f16 - cSPTA SH3 domain
- 1uue, 1e7o, 1g2b, 1aey, 1tuc, 1tud - cSPTA SH3 domain (mutant) – NMR
- Spectrin β1
- Spectrin β2
- 3edv – hSPTB2 repeats 14-16
- Spectrin β3
- Spectrin β
- Spectrin R16
- 3e5m6s – SPT - Escherichia coli
- 3e5m6s – SPT - Escherichia coli
References
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