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Figure 1.
Figure 1. CaM-binding domain of MARCKS-related proteins. a,
Schematic diagram of mouse MARCKS domain structure. The
conventional full sequence of CaM-binding domain including basic
cluster regions is shown. Sequences of 19-residue peptide are
conserved among human, mouse, rat and bovine. Residues whose
electron densities were observed in the present structure are
underlined. Residues interacting with CaM are colored green for
hydrophobic residues, red for basic residues and blue for serine
residues. Key hydrophobic residues that interact either solely
with N- or C-lobe of CaM -- Phe157 and Leu159 -- are boxed. The
known phosphorylation sites are labeled with 'P'. b, Alignment
of sequences of CaM-binding region of proteins with similar
sequence characteristics. Key hydrophobic residues that may
interact with hydrophobic pockets or surfaces are boxed.
Conserved basic and hydrophobic residues are shown in red and
green, respectively. Sequences shown are MLP (residues 87
-100)2, DAKAP200 (residues 128 -141)39, ADD1 (residues 717
-737)26, AKAP79 (residues 31 -52)28, RALA (residues 183 -200)27
and GRK (residues 20 -39)29.
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