PMID: 9659401Jul 11, 1998Paper

Motifs involved in interchain binding at the tail-end of spectrin

Biochimica Et Biophysica Acta
A VielD Branton

Abstract

Segments 20-22 of alpha-spectrin and 1-3 of beta-spectrin are required for high avidity interchain binding at the tail-end of the molecule. Here, sequence analysis guided by the crystal structure of spectrin's repeating segments was used to redefine the boundaries of a repetitive beta segment that is critical for interchain binding and demonstrate the contribution of non-repetitive spectrin segments in high avidity interchain binding. Our results show that several motifs together are required for high avidity binding, indicating that interchain binding at the tail-end of the spectrin molecule depends on the long distance coordination of several different elements. We also explored the role of unusual motifs contained in beta segments involved in interchain binding. A row of basic residues and a row of small hydrophobic residues were found not to be required for interchain binding, suggesting that their conservation among species reflects functions unrelated to interchain binding. The octamer between segments beta 2 and beta 3 that maintains a specific register between true binding sites was found to have an indirect role in interchain binding by stabilizing neighboring segments. A 5-residue domain in segment beta 2 (EKPPK) was ...Continue Reading

References

Jul 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·T J ByersD Branton
Jan 1, 1995·The Journal of Cell Biology·H DengD Branton
Nov 8, 1994·Proceedings of the National Academy of Sciences of the United States of America·A Viel, D Branton
Jan 15, 1994·The Biochemical Journal·M P Williamson
Jan 20, 1993·Journal of Molecular Biology·A A Adzhubei, M J Sternberg
Feb 1, 1996·Current Opinion in Cell Biology·A Viel, D Branton

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Citations

Apr 28, 2000·European Journal of Biochemistry·L GalluzziM C Lecomte
Jan 11, 2011·Biochimica Et Biophysica Acta·Xiuli AnNarla Mohandas
Jul 21, 2009·Biochemical Society Transactions·Anthony J Baines

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