Alpha-actinin and spectrin structures: an unfolding family story.
In red blood cells, the integrity of the spectrin network is essential for normal cell shape and elasticity. To understand the molecular basis for spectrin's mechanical properties, one must determine how spectrin subunits interact with each other. The newly described crystallographic structures of two consecutive homologous repeats of human alpha-actinin, a member of the spectrin superfamily, shed new light on alpha-actinin interchain binding properties. Here I present evidence that interchain binding at the tail end of the spectrin molecule is likely to occur via a mechanism similar to that observed for alpha-actinin.
Viel
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Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Bldg. 149, 13th Street, Charlestown, MA 02129, USA.alain.viel@cbrc2.mgh.harvard.edu
D000185:Actinin / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013049:Spectrin / Q000737:chemistry*
D000185:Actinin; D013049:Spectrin