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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Mapping the tropomyosin isoform 5 binding site on human erythrocyte tropomodulin: further insights into E-Tmod/TM5 interaction.

Actin protofilaments in the erythrocyte membrane skeleton are uniformly approximately 37nm. This length may be in part attributed to a "molecular ruler" made of erythrocyte tropomodulin (E-Tmod) and tropomyosin (TM) isoforms 5 or 5b. We previously mapped the E-Tmod binding site to TM5 N-terminal heptad repeat residues "a" (I(7), I(14)), "d" (V(10)) and "f" (R(12)). We now map the TM5 binding site to E-Tmod residues at L(116), E(117) and/or E(118) by identifying among 35 deletion clones and a series of point mutations that no longer bind to human TM5 and rat TM5b. Upstream residues 71-104 contain an actin binding site. The N-terminal "KRK ring" may participate in balancing electrostatic force with hydrophobic interaction in dimerization of TM and its binding to E-Tmod.[1]

References

  1. Mapping the tropomyosin isoform 5 binding site on human erythrocyte tropomodulin: further insights into E-Tmod/TM5 interaction. Vera, C., Lao, J., Hamelberg, D., Sung, L.A. Arch. Biochem. Biophys. (2005) [Pubmed]
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