Biology:Spectrin repeat

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Spectrin repeat
PDB 1aj3 EBI.jpg
Structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil.[1]
Identifiers
SymbolSpectrin
PfamPF00435
InterProIPR002017
PROSITEPDOC50083
SCOP21aj3 / SCOPe / SUPFAM
CDDcd00176

Spectrin repeats[2] are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin, dystrophin and more recently the plakin family. The spectrin repeat forms a three-helix bundle. These conform to the rules of the heptad repeat. Spectrin repeats give rise to linear proteins. This however may be due to sample bias in which linear and rigid structures are more amenable to crystallization. There are hints however, that some proteins harbouring spectrin repeats may also be flexible. This is most likely due to specifically evolved functional purposes.

Human proteins containing this domain

ACTN1; ACTN2; ACTN3; ACTN4; AKAP6; SYNE3; CATX-15; DMD; DRP2; DST; KALRN; MACF1; MCF2L; SPTA1; SPTAN1; SPTB; SPTBN1; SPTBN2; SPTBN4; SPTBN5; SYNE1; SYNE2; TRIO; UTRN;

References

  1. "Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil". J. Mol. Biol. 273 (3): 740–51. October 1997. doi:10.1006/jmbi.1997.1344. PMID 9356261. 
  2. "Crystal structure of the repetitive segments of spectrin". Science 262 (5142): 2027–2030. 1993. doi:10.1126/science.8266097. PMID 8266097. 

Further reading

  • "The spectrin repeat: a structural platform for cytoskeletal protein assemblies". FEBS Lett. 513 (1): 119–23. February 2002. doi:10.1016/S0014-5793(01)03304-X. PMID 11911890. 
  • "Evolution of the spectrin repeat". BioEssays 19 (9): 811–7. September 1997. doi:10.1002/bies.950190911. PMID 9297972. 
  • Al-Jassar, C; Knowles, T; Jeeves, M; Kami, K; Behr, E; Bikker, H; Overduin, M; Chidgey, M (Jul 2, 2011). "The Nonlinear Structure of the Desmoplakin Plakin Domain and the Effects of Cardiomyopathy-Linked Mutations.". Journal of Molecular Biology 411 (5): 1049–61. doi:10.1016/j.jmb.2011.06.047. PMID 21756917.