User:Michael Roberts/BIOL115 CaM
From Proteopedia
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The EF hand motif is present in a many proteins and it commonly bestows the ability to bind Ca2+ ions. It was first identified in parvalbumin, a muscle protein. Here we will have a look at the Ca2+-binding protein [[calmodulin]], which possesses four EF hands. Calmodulin and its isoform, troponinC, are important intracellular Ca2+-binding proteins. | The EF hand motif is present in a many proteins and it commonly bestows the ability to bind Ca2+ ions. It was first identified in parvalbumin, a muscle protein. Here we will have a look at the Ca2+-binding protein [[calmodulin]], which possesses four EF hands. Calmodulin and its isoform, troponinC, are important intracellular Ca2+-binding proteins. | ||
| - | The structure | + | |
| + | The structure below, obtained by X-ray crystallography, represents the Ca2+-binding protein calmodulin. It has a dumbell-shaped structure with two identical lobes connected by a central alpha-helix. Each lobe comprises three a helices joined by loops. A helix-loop-helix motif forms the basis of each EF hand. | ||
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The wireframe view shows us all the atoms, but this can be too much detail if we're mainly interested ion the overall structure of the protein. This next veiw takes us right doewn to a minimal representation that simply traces the <scene name='User:Michael_Roberts/BIOL115_CaM/Backbone/1'>"backbone" </scene>of the protein. The backbone includes the peptide linkages between each amino acid, along with the a-carbon atoms to which R-groups are attached. | The wireframe view shows us all the atoms, but this can be too much detail if we're mainly interested ion the overall structure of the protein. This next veiw takes us right doewn to a minimal representation that simply traces the <scene name='User:Michael_Roberts/BIOL115_CaM/Backbone/1'>"backbone" </scene>of the protein. The backbone includes the peptide linkages between each amino acid, along with the a-carbon atoms to which R-groups are attached. | ||
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| - | Anything in this section will appear adjacent to the 3D structure and will be scrollable. | ||
| - | </StructureSection> | ||
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Let us color the two main forms of regular <scene name='Sandbox_LUBIOL115/Structure_plus_ca/1'>secondary structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow. | Let us color the two main forms of regular <scene name='Sandbox_LUBIOL115/Structure_plus_ca/1'>secondary structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow. | ||
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{{Template:ColorKey_Strand}}, | {{Template:ColorKey_Strand}}, | ||
{{Template:ColorKey_Turn}}. | {{Template:ColorKey_Turn}}. | ||
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| + | End of section | ||
| + | </StructureSection> | ||
Revision as of 10:28, 12 April 2013
Sequence and structure of EF hands
The EF hand motif is present in a many proteins and it commonly bestows the ability to bind Ca2+ ions. It was first identified in parvalbumin, a muscle protein. Here we will have a look at the Ca2+-binding protein calmodulin, which possesses four EF hands. Calmodulin and its isoform, troponinC, are important intracellular Ca2+-binding proteins.
The structure below, obtained by X-ray crystallography, represents the Ca2+-binding protein calmodulin. It has a dumbell-shaped structure with two identical lobes connected by a central alpha-helix. Each lobe comprises three a helices joined by loops. A helix-loop-helix motif forms the basis of each EF hand.
Click on the 'green links' in the text in the scrollable section below to examine this molecule in more detail.
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