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1-16 Motif


  • This unique motif is created because of its unique binding geometry identified in the NMR study.
  • The NMR structure of Calmodulin-dependent Kinase Kinase (CaMKK) peptide and Calmodulin has been studied (Osawa et al, 1999). The structure is unlike any other ones studied before. First of all, the orientation of binding (N-terminal of peptide binding to N-terminal domain of calmodulin) is reverse of typical binding orientation of calmodulin-binding peptides (N-termnial of peptide binding to C-terminal domain of calmodulin). For more information on CaMKK, click here.
  • Also unique is the fact that the key anchor residues are 14 residues apart instead of 12 or 8 as in 1-14 and 1-10 motifs. This motif is also distinctive in that the tail region loops back on itself within one of the domains in calmodulin.

Subclasses

1-16 (FILVW)xxxxxxxxxxxxxx(FILVW)
  • Residues within parentheses may substitute for each other.

Data

Average of this Class and Links to Graphs

Sequence Alignment, Data and Homologs

1-16

CaMKK with Ca2+-Calmodulin
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