EF hand: Difference between revisions

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The 3D structure of EF hands is depicted in the scenes below, which show three examples of EF hand proteins. [[Parvalbumin]] is a monomeric protein that has a pair of EF hands, [[calmodulin]] is a monomer with two pairs, and [[Calcium-dependent protein kinase]] is a monomer with a protein kinase catalytic domain and its calcium-binding domain has two pairs of EF hands. As shown in these examples EF hands often occur in interacting pairs, which enables the cooperative binding of calcium ions.

Scenes ~~numbered~~ 1 are the default scenes showing the proteins in cartoon with Ca2+ in green space fill. The calcium binding domain of CDPK is blue and the kinase catalytic domain is in gold and has an ATP analog (sticks in CPK colors) bound in its active site.

'''Scenes 1''' are the default scenes showing the proteins in cartoon with Ca2+ in green space fill. The calcium binding domain of CDPK is blue and the kinase catalytic domain is in gold and has an ATP analog (sticks in CPK colors) bound in its active site.

Scenes ~~numbered~~ 2 show pairs of EF hands in each protein, one in blue and one in gold, which are linked by the sequence shown in orchid.

'''Scenes 2''' show pairs of EF hands in each protein, one in blue and one in gold, which are linked by the sequence shown in orchid.

Scenes ~~numbered~~ 3 isolate one EF hand: the eponymous EF hand of parvalbumen, EF hand I (they are numbered I-IV) in calmodulin, and EF hand IV of CDPK.

'''Scenes 3''' isolate one EF hand: the eponymous EF hand of parvalbumen, EF hand I (they are numbered I-IV) in calmodulin, and EF hand IV of CDPK.

Scenes ~~numbered~~ 4 show the calcium binding loops in the same orientation. The protein backbone is shown as a trace and the sidechains of residues that provide ligands are shown in ball and stick. The five oxygen atoms that form the the base of the bipyramid are contributed by four residues (positions 3, 5, 7, and 12) distributed around the equator of the calcium ion, one pyramid point ("north" in the scenes) is the oxygen from water, and the "south" point is the side chain oxygen from the invariant D at position 1 in the motif.

'''Scenes 4''' show the calcium binding loops in the same orientation. The protein backbone is shown as a trace and the sidechains of residues that provide ligands are shown in ball and stick. The five oxygen atoms that form the the base of the bipyramid are contributed by four residues (positions 3, 5, 7, and 12) distributed around the equator of the calcium ion, one pyramid point ("north" in the scenes) is the oxygen from water, and the "south" point is the side chain oxygen from the invariant D at position 1 in the motif.

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 The 3D structure of EF hands is depicted in the scenes below, which show three examples of EF hand proteins. [[Parvalbumin]] is a monomeric protein that has a pair of EF hands, [[calmodulin]] is a monomer with two pairs, and [[Calcium-dependent protein kinase]] is a monomer with a protein kinase catalytic domain and its calcium-binding domain has two pairs of EF hands. As shown in these examples EF hands often occur in interacting pairs, which enables the cooperative binding of calcium ions.
-Scenes numbered 1 are the default scenes showing the proteins in cartoon with Ca<sup>2+</sup> in green space fill. The calcium binding domain of CDPK is blue and the kinase catalytic domain is in gold and has an ATP analog (sticks in CPK colors) bound in its active site.<br>
+'''Scenes 1''' are the default scenes showing the proteins in cartoon with Ca<sup>2+</sup> in green space fill. The calcium binding domain of CDPK is blue and the kinase catalytic domain is in gold and has an ATP analog (sticks in CPK colors) bound in its active site.<br>
-Scenes numbered 2 show pairs of EF hands in each protein, one in blue and one in gold, which are linked by the sequence shown in orchid.<br>
+'''Scenes 2''' show pairs of EF hands in each protein, one in blue and one in gold, which are linked by the sequence shown in orchid.<br>
-Scenes numbered 3 isolate one EF hand: the eponymous EF hand of parvalbumen, EF hand I (they are numbered I-IV) in calmodulin, and EF hand IV of CDPK.<br>
+'''Scenes 3''' isolate one EF hand: the eponymous EF hand of parvalbumen, EF hand I (they are numbered I-IV) in calmodulin, and EF hand IV of CDPK.<br>
-Scenes numbered 4 show the calcium binding loops in the same orientation. The protein backbone is shown as a trace and the sidechains of residues that provide ligands are shown in ball and stick. The five oxygen atoms that form the the base of the bipyramid are contributed by four residues (positions 3, 5, 7, and 12) distributed around the equator of the calcium ion, one pyramid point ("north" in the scenes) is the oxygen from water, and the "south" point is the side chain oxygen from the invariant D at position 1 in the motif.
+'''Scenes 4''' show the calcium binding loops in the same orientation. The protein backbone is shown as a trace and the sidechains of residues that provide ligands are shown in ball and stick. The five oxygen atoms that form the the base of the bipyramid are contributed by four residues (positions 3, 5, 7, and 12) distributed around the equator of the calcium ion, one pyramid point ("north" in the scenes) is the oxygen from water, and the "south" point is the side chain oxygen from the invariant D at position 1 in the motif.
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