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Figure 3.
Fig. 3. Surface representations of EF-hand protein-target
interactions. A, the solution structure of cTnC bound to cTnI .
cTnC was found to have bend, azimuth, and twist angles of
70°, 30°, and  29°,
respectively. B, the x-ray structure of sTnC bound to
sTnI-(1-47) (11). The orientation of sTnC domains is defined by
bend, azimuth, and twist angles of 93°, 162°,
and 25°, respectively. C, the crystal structure of four
Ca^2+-loaded sTnC (36). The orientation of sTnC domains is
defined by bend, azimuth, and twist angles of 12°, 94°,
and 3°,
respectively. The N- and C-terminal domains of TnC are shown in
gold and red, respectively. TnI peptides are shown in magenta
and blue. Superposition of TnC C-terminal domains was used to
provide similar orientations. D, the NMR structure of
Ca^2+-bound CaM complexed with the myosin light chain kinase
peptide (37). The orientation of CaM domains is defined by bend,
azimuth, and twist angles of 111°, 95°,
and 68°,
respectively. The N- and C-terminal domains of CaM are shown in
gold and red, respectively. The CaM-bound myosin light chain
kinase peptide is shown in blue. Superposition of the CaM
C-terminal domain and the TnC C-terminal domain was used to
provide similar orientations.
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