Spectrin: Difference between revisions
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New page: left|200px|thumb|Crystal Structure of Spectrin [[3lbx]] {{STRUCTURE_3lbx| PDB=3lbx | SIZE=300| SCENE= |right|CAPTION=Spectrin 3lbx }} |
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[[ | <StructureSection load='3lbx' size='340' side='right' caption='Human spectrin α (grey) and β1 chain (green) [[3lbx]]' scene=''> | ||
== 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 α2''' is expressed highly in heart muscle cells<ref>PMID:15360127</ref>. | |||
*'''Spectrin β2''' is associated with GABA receptor at dendritic synapses<ref>PMID:36604600</ref>. | |||
*'''Spectrin β4''' is associated with GABA receptor at axon initial segment synapses. | |||
*'''Spectrin R16''' is spectrin α first repeat domain<ref>PMID:10481916</ref>. | |||
== 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>. | |||
== 3D Structures of Spectrin == | |||
[[Spectrin 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | |||
