2spc

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CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRINCRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN

Structural highlights

2spc is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPTCA_DROME] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.

Crystal structure of the repetitive segments of spectrin.,Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D Science. 1993 Dec 24;262(5142):2027-30. PMID:8266097[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Lee JK, Coyne RS, Dubreuil RR, Goldstein LS, Branton D. Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster. J Cell Biol. 1993 Dec;123(6 Pt 2):1797-809. PMID:8276898
  2. ↑ Dubreuil R, Byers TJ, Branton D, Goldstein LS, Kiehart DP. Drosophilia spectrin. I. Characterization of the purified protein. J Cell Biol. 1987 Nov;105(5):2095-102. PMID:3680372
  3. ↑ Sisson JC, Field C, Ventura R, Royou A, Sullivan W. Lava lamp, a novel peripheral golgi protein, is required for Drosophila melanogaster cellularization. J Cell Biol. 2000 Nov 13;151(4):905-18. PMID:11076973
  4. ↑ Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D. Crystal structure of the repetitive segments of spectrin. Science. 1993 Dec 24;262(5142):2027-30. PMID:8266097

2spc, resolution 1.80Å

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