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. Author manuscript; available in PMC: 2012 Oct 28.
Published in final edited form as: J Mol Biol. 2011 Sep 8;413(3):712–725. doi: 10.1016/j.jmb.2011.08.059

Table 2.

α-Actinin is capable of binding to a relatively diverse range of sequences. Sequence alignment of residues associated with proteins involved in binding Act-EF34, highlighting the proposed '1-4-5-8' motif. Numbers indicate positions of the hydrophobic residues involved in binding with numbering starting from the first hydrophobic residue. The residue in palladin mutated in FX is highlighted in red, while the leucines mutated in the binding motif are in blue.

Protein Residues Act2-EF34 Binding Site
'1--45--8'
Palladin 235–251 graphic file with name nihms324539t1.jpg
Myotilin 89–105 NQSPASFLSSILPSQPD
Myopalladin 822–837 IQNPVAFLSSVLPSLP
Titin ZR1 424–439      AVATVVAAVDMARVRE
     ZR3 519–534      FVPKVVISAAKAKEQE
     ZR7 659–674      AVATVVAAVDQARVRE
Actinin N-term 259–281 AETAANRICKVLAVNQE