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Spectrin repeat

From Wikipedia, the free encyclopedia
Spectrin repeat
Structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil.[1]
Identifiers
SymbolSpectrin
PfamPF00435
InterProIPR002017
PROSITEPDOC50083
SCOP21aj3 / SCOPe / SUPFAM
CDDcd00176
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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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

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  1. ^ Pascual J, Pfuhl M, Walther D, Saraste M, Nilges M (October 1997). "Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil". J. Mol. Biol. 273 (3): 740–51. doi:10.1006/jmbi.1997.1344. PMID 9356261.
  2. ^ Harrison SC, Yan Y, Winograd E, Viel A, Cronin T, Branton D (1993). "Crystal structure of the repetitive segments of spectrin". Science. 262 (5142): 2027–2030. doi:10.1126/science.8266097. PMID 8266097.

Further reading

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