NDLI: Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.

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Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.

Content Provider	Scilit
Author	Byers, T. J. Husain-Chishti, A. Dubreuil, R. R. Branton, D. Goldstein, L. S.
Copyright Year	1989
Description	Journal: Journal of Cell Biology We used chicken alpha spectrin as a ligand probe to isolate Drosophila beta spectrin cDNA sequences from a lambda gt11 expression library. Analysis of 800 residues of deduced amino acid sequence at the amino-terminal end revealed a strikingly conserved domain of integral of 230 residues that shows a high degree of sequence similarity to the amino-terminal domains of alpha actinin and dystrophin. This conserved domain constitutes a new diagnostic criterion for spectrin-related proteins and allows the known properties of one of these proteins to predict functional properties of the others. The conservation of the amino-terminal domain, and other regions in spectrin, alpha actinin, and dystrophin, demonstrates that a common set of domains were linked in different combinations through evolution to generate the distinctive members of the spectrin superfamily.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115807/pdf http://jcb.rupress.org/content/109/4/1633.full.pdf
ISSN	00221295
DOI	10.1083/jcb.109.4.1633
Journal	Journal of Cell Biology
Issue Number	4
Volume Number	109
Language	English
Publisher	Rockefeller University Press
Publisher Date	1989-10-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Cell Biology Biochemistry and Molecular Biology Amino Terminal Terminal Domain Alpha Actinin
Content Type	Text
Resource Type	Article
Subject	Physiology

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