Spectrin: Difference between revisions
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{{STRUCTURE_3lbx| PDB=3lbx | SIZE=300| SCENE= |right|CAPTION=Spectrin α (grey) and β chain (green) [[3lbx]] }} | {{STRUCTURE_3lbx| PDB=3lbx | SIZE=300| SCENE= |right|CAPTION=Spectrin α (grey) and β chain (green) [[3lbx]] }} | ||
[[Spectrin]] forms scaffolding in plasma membranes and cytoskeletal structure. It interacts with actin at either end of its tetramer. The SPT dimer is formed by association of | [[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. | ||
== 3D Structures of Spectrin == | == 3D Structures of Spectrin == | ||
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**[[2spc]] – SPT fragment - ''Drosophila melanogaster'' | **[[2spc]] – SPT fragment - ''Drosophila melanogaster'' | ||
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== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 15:12, 30 August 2016
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.
3D Structures of Spectrin3D Structures of Spectrin
Updated on 30-August-2016
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