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. 2009 Mar 6;284(10):6446–6454. doi: 10.1074/jbc.M807401200

TABLE 2.

Comparison of helix orientations in EF-hand proteins

Interhelical angles are shown in degrees with interhelical distances shown in Å in parentheses. Calculations refer to the following structures. Ca-CaM is Ca2+ -loaded target-free calmodulin (PDB code 1EXR, 1.00 Å) (67), IQ-Ca-CaM is Ca2+ -loaded calmodulin bound to the voltage-gated Ca2+ channel Cav1.2 IQ-motif (PDB code 2F3Y, 1.45 Å) (81), and apoCaM is apoCa2+ target-free calmodulin (PDB code 1CFD, NMR) (82), with helix I defined as residues 6-18, helix II as residues 29-38, helix III as residues 45-54, and helix IV as residues 65-74. Interhelical angles for the Nav1.2 CTD are the averages with S.D. for the structural ensemble.

Molecule Helix II Helix III Helix IV
Helix I
Ca-CaM 85 (20.4) −134 (25.5) 91 (14.6)
IQ-Ca-CaM 92 (18.3) −161 (21.9) 117 (10.1)
ApoCaM 136 (12.9) −93 (21.2) 126 (11.9)
Nav1.2 CTD 152 ± 2 (10.9 ± 0.1) −103 ± 6 (20.9 ± 0.3) 143 ± 1 (15.7 ± 0.2)
Helix II
Ca-CaM 83 (10.1) −20 (16.7)
IQ-Ca-CaM 107 (11.2) −41 (18.6)
ApoCaM 125 (11.9) −49 (12.9)
Nav1.2 CTD 100 ± 5 (10.8 ± 0.4) −46 ± 2 (13.4 ± 0.1)
Helix III
Ca-CaM 65 (15.3)
IQ-Ca-CaM 80 (16.5)
ApoCaM 129 (14.1)
Nav1.2 CTD 98 ± 6 (14.4 ± 0.4)