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| {{STRUCTURE_3lbx| PDB=3lbx | SIZE=300| SCENE= |right|CAPTION=Human spectrin α (grey) and β1 chain (green) [[3lbx]] }}
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| | <StructureSection load='3lbx' size='340' side='right' caption='Human spectrin α (grey) and β1 chain (green) [[3lbx]]' scene=''> |
| == Function == | | == Function == |
| [[Spectrin]] forms scaffolding in plasma membranes and cytoskeletal structure. It interacts with actin at either end of its tetramer<ref>PMID:17060500</ref>. 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. | | [[Spectrin]] forms scaffolding in plasma membranes and cytoskeletal structure. It interacts with actin at either end of its tetramer<ref>PMID:17060500</ref>. 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. |
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| == Disease == | | == Disease == |
| Mutations in SPT α are found in patients with hereditary elliptocytosis<ref>PMID:2346784</ref>. SPT β deficiency is found in hereditary spherocytosis<ref>PMID:9714702</ref>. | | Mutations in SPT α are found in patients with hereditary elliptocytosis<ref>PMID:2346784</ref>. SPT β deficiency is found in hereditary spherocytosis<ref>PMID:9714702</ref>. |
| | | </StructureSection> |
| == 3D Structures of Spectrin == | | == 3D Structures of Spectrin == |
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| **[[3lbx]] – hSPTA1+hSPTB1 – human<br /> | | **[[3lbx]] – hSPTA1+hSPTB1 – human<br /> |
| **[[3i9q]], [[2rot]], [[2pqh]], [[2oaw]], [[2nuz]], [[1u06]] - cSPTA1 SH3 domain – chicken<br /> | | **[[3i9q]], [[2rot]], [[2oaw]], [[2nuz]], [[1u06]] - cSPTA1 SH3 domain – chicken<br /> |
| **[[2jm8]], [[2jm9]], [[2cdt]], [[2f2v]], [[2f2w]], [[2f2x]] - cSPTA1 SH3 domain (mutant)<br /> | | **[[2jm8]], [[2jm9]], [[2cdt]], [[2f2v]], [[2f2w]], [[2f2x]] - cSPTA1 SH3 domain (mutant)<br /> |
| **[[2jma]], [[2jmc]] - cSPTA1 SH3 domain (mutant)+P41 peptide<br /> | | **[[2jma]], [[2jmc]] - cSPTA1 SH3 domain (mutant)+P41 peptide<br /> |
| Function
Spectrin 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.
Disease
Mutations in SPT α are found in patients with hereditary elliptocytosis[2]. SPT β deficiency is found in hereditary spherocytosis[3].
- ↑ 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:https://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:https://dx.doi.org/10.1006/bcmd.1998.0190
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3D Structures of Spectrin
Updated on 24-November-2016
{"openlevels":0}
- Spectrin α1
- 3lbx – hSPTA1+hSPTB1 – human
- 3i9q, 2rot, 2oaw, 2nuz, 1u06 - cSPTA1 SH3 domain – chicken
- 2jm8, 2jm9, 2cdt, 2f2v, 2f2w, 2f2x - cSPTA1 SH3 domain (mutant)
- 2jma, 2jmc - cSPTA1 SH3 domain (mutant)+P41 peptide
- 2rmo, 1neg, 1m8m - cSPTA1 SH3 domain – NMR
- Spectrin α2
- 3f31 – hSPTA2 tetramerization domain
- 1qkw – cSPTA2 SH3 domain (mutant)
- 2fot - SPTA2+calmodulin – bovine
- 3fb2 – hSPTA2 repeats 15-16
- 3thk - SPTA2 SH3 domain + polypeptide - rat
- 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
- Spectrin β1
- Spectrin β2
- 3edv – hSPTB2 repeats 14-16
- Spectrin β3
- 1wyq – hSPTB3 CH domain – NMR
- 1wjm – hSPTB3 – NMR
- Spectrin β
- 1bkr, 1aa2 – hSPTB CH domain
- 1mph – SPTB Pleckstrin Homology domain – NMR
- 1dro - mSPTB PH domain – NMR – mouse
- 1btn – mSPTB+inositol phosphate
- 2spc – SPT fragment - Drosophila melanogaster
References
