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Figure 2.
Figure 2. a, Schematic drawing of interacting residues between
Ca ^2+ /CaM and CaMKK peptide. Residues in N-domain and
C-domain are colored in cyan and violet, respectively. Key
residues of the CaMKK peptide anchoring the hydrophobic pocket
in each domain, Trp 444 and Phe 459, are shown in green. b,
Portions of ^13 C/F[3]-filtered ^13 C/F[1]-edited HMQC-NOESY
spectrum ^24 showing intermolecular NOEs between CaM and the
CaMKK peptide. Stereo drawing of the key residues of CaMKK
peptide in the hydrophobic pocket of c, N-domain and
d,C−domain. esidues within 5 Šof the key residues, Trp
444 and Phe 459, are shown. N, O and S atoms are colored in
blue, red and yellow, respectively, while C atoms of N- and
C-domain of CaM and CaMKK are shown in cyan, violet and gray,
respectively. Diagrams (c) and (d) were generated using the
program MOLMOL^55.
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