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Figure 1.
Figure 1. The profilin ligands used in the current study. (a)
A diagram of the structures of the profilin 2a ligands, mDia1
and VASP. For mDia1, the domains are as follows: GBD,
Rho-GTPase-binding domain; DID, diaphanous inhibitory domain;
DD, dimerisation domain; CC, coiled-coil domain; FH1, formin
homology domain 1; FH2, formin homology domain 2; DAD,
diaphanous autoinhibitory domain. The regions N-terminal to the
FH1 domain have been referred to in the literature as the FH3
domain. For VASP, the EVH1 domain, the proline-rich domain, and
the EVH2 domain are indicated. The EVH2 domain contains a WH2
domain (dark grey), an F-actin binding domain (light grey), and
a tetramerisation domain (white). The sequences of the peptides
used in this study are shown below the profilin-binding domains.
(b) The sequence of the FH1 domain of mDia1, which has 13 highly
homologous proline-rich repeats arranged in tandem. The peptide
used in this study, containing two binding motifs, is underlined.
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