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Figure 2.
FIGURE 2. An N-domain structure comparison between Mlc1p
(PDB entry 1M46 (10), green) and apoCaM (PDB entry 1CFD, red).
Structure superposition was performed considering backbone atoms
belonging to residues of the four helices: 5-14, 26-32, 40-48,
and 61-68 (Mlc1p) and 10-19, 31-37, 45-53, and 65-72 (apoCaM).
Highlighted are residues that confer special structural features
to Mlc1p; Leu-75, that is added to the hydrophobic core of the
N-lobe, and Thr-78 and Asn-37, which interact through hydrogen
bonds. Asn-37 is a key residue for the regulation of the
interaction between the N-lobe and IQ-spanning peptides. B,
chemical shift index for C  and ^3J[HNH ]measured for helix D
and helix D'. C, strips from ^13C- and ^15N-edited NOESY spectra
showing the interaction between Thr-78 and Asn-37 and several
NOEs from Leu-75 methyl groups.
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