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].
| |
3D Structures of Spectrin3D Structures of Spectrin
Updated on 05-November-2020
{"openlevels":0}
- Spectrin α1; Domains – N-terminal tetramerization 1-156; SH3 969-1025; C-terminal tetramerization 1902-2084
- 3lbx – hSPT a chain N-terminal tetramerization domain +hSPT b chain C-terminal tetramerization domain – human
- 2rot, 2oaw, 2nuz, 1u06 - cSPT a chain SH3 domain – chicken
- 2jm8, 2jm9, 2cdt, 2f2v, 2f2w, 2f2x, 3i9q - cSPT a chain SH3 domain (mutant)
- 2rmo, 1neg, 1m8m - cSPT a chain SH3 domain – NMR
- 2jma, 2jmc - cSPT a chain SH3 domain (mutant)+P41 peptide
- Spectrin α2
- 3f31 – hSPT a2 chain N-terminal tetramerization domain
- 3fb2 – hSPT a2 chain repeats 15-16 1337-1544
- 5fw9, 5fwb, 5fwc, 5ihi, 5ihk, 5ihn – hSPT a2 chain SH3 domain (mutant)
- 2fot - SPT a2 chain calmodulin-binding domain 1172-1211 +calmodulin – bovine
- 3thk - SPT a2 chain SH3 domain + polypeptide - rat
- 1qkw – cSPT a2 chain SH3 domain (mutant)
- Spectrin α
- 1owa - hSPT a chain N-terminal tetramerization domain – NMR
- 5j4o - hSPT a chain repeats 16-17 1599-1826
- 2kr3, 4f17, 4f16 - cSPT a chain SH3 domain
- 1e6g, 1e6h, 1hd3, 1qkx, 1pwt, 1bk2, 1shg, 1h8k, 3ngp, 3m0p, 3m0q, 3m0r, 3m0s, 3m0t, 3m0u - cSPT a chain SH3 domain (mutant)
- 1uue, 1e7o, 1g2b, 1aey, 1tuc, 1tud - cSPT a chain SH3 domain (mutant) – NMR
- 2lj3 - cSPT a chain SH3 domain – NMR
- 1u4q – cSPT a chain repeats 15-17 1662-1982
- 1u5p - cSPT a chain repeats 15-16 1662-1876
- 1cun - cSPT a chain repeats 16-17 (mutant) 1771-1982
- 1aj3 - cSPT a chain repeat 16 1772-1869 - NMR
- Spectrin β1
- 3kbt, 3kbu - hSPT β1 chain repeats 13-15 1583-1906 +ankyrin
- 3f57, 3edu - hSPT β1 chain repeats 14-15 1686-1906
- 1s35 – hSPT β1 chain repeats 8-9 1063-1275 (mutant)
- Spectrin β2
- 3edv – hSPT β2 chain repeats 14-16 1697-2015
- Spectrin β3
- 1wyq – hSPT β3 chain 2nd CH domain – NMR
- 1wjm – hSPT β3 chain PH domain 2199-2328 – NMR
- 6anu - hSPT β3 chain actin binding domain 1-284 + actin - Cryo EM
- Spectrin β
- 1bkr, 1aa2 – hSPT β chain 2nd CH domain 178-291
- 1dro, 1mph - mSPT β chain PH domain 2199-2304 – NMR – mouse
- 1btn – mSPT β chain PH domain +inositol phosphate
- 2spc – SPT fragment 1391-1497 - Drosophila melanogaster
- Spectrin R16
- 5m6s – SPT - Escherichia coli
ReferencesReferences
- ↑ Das A, Base C, Dhulipala S, Dubreuil RR. Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway. J Cell Biol. 2006 Oct 23;175(2):325-35. PMID:17060500 doi:http://dx.doi.org/10.1083/jcb.200602095
- ↑ Coetzer T, Palek J, Lawler J, Liu SC, Jarolim P, Lahav M, Prchal JT, Wang W, Alter BP, Schewitz G, et al.. Structural and functional heterogeneity of alpha spectrin mutations involving the spectrin heterodimer self-association site: relationships to hematologic expression of homozygous hereditary elliptocytosis and hereditary pyropoikilocytosis. Blood. 1990 Jun 1;75(11):2235-44. PMID:2346784
- ↑ Dhermy D, Galand C, Bournier O, Cynober T, Mechinaud F, Tchemia G, Garbarz M. Hereditary spherocytosis with spectrin deficiency related to null mutations of the beta-spectrin gene. Blood Cells Mol Dis. 1998 Jun;24(2):251-61. PMID:9714702 doi:http://dx.doi.org/10.1006/bcmd.1998.0190
