Calmodulin: PDB 1CDM
Structure of bovine brain calmodulin, with the calmodulin-binding segment (target sequence) of calmodulin-dependent protein kinase II, solved by W. Meador & F. Quiocho, 1994.
Recommended display options:
Color chain to distinguish calmodulin from its target peptide.
Display as ribbons or cartoon
to show the largely a-helical structure of both proteins.
Note how calmodulin
(blue) wraps around the target peptide (green).
Select hetero-ligand, display as spacefill, & color CPK to visualize Ca++.
Question: How many Ca++ ions are bound to calmodulin?
Drag the image, and observe the helix-loop-helix motif of each Ca++
binding site.
Type into the command line select
met*a,
enter, and then change display to spacefill,
with color CPK, to view the cluster of
methionine residues that forms a hydrophobic pocket at each end of calmodulin.
Select leu299
and change its display to view the position of a conserved hydrophobic residue
in the target protein. This residue, which may be either Trp or Leu, is
essential for sensitivity of some kinases to calmodulin.
Now, to get a clearer view of one Ca++
binding site, select
all, and then hide
selected.
Type
into the command line select 1-40a, enter, and display as ribbons.
Select
ca1 (calcium #1) & display as spacefill.
Enter select 20-26a, display as ball & stick, and color CPK. Hold down the shift while left-dragging to zoom in.
Identify
amino acids that
interact with Ca++. (Hint: May include anionic amino acids above).
Question:
What atoms of
what chemical groups interact with Ca++?
Return to
Lecture Notes
on Ca++ Signals
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