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OTHERS


  • Sequences in this family do not belong to any of the previously described motifs (IQ Motif, 1-14 Motif, 1-10 Motif or 1-16 Motif).
  • We propose the definition of two other groups: the 1-12 motif, for which the bulky hydrophobic residues (FILVW) are separated by 10 residues, and the basic motif, in which there are several lysine or arginine residues occurring within the calmodulin binding sequence.
  • There is currently no high resolution structure available for calmodulin binding to a 1-12 motif, although as hydrophobic residues normally play an essential role in most calmodulin-target interactions, it is highly possible that such a motif would be employed in some cases.
  • In sequences categorized here as basic motifs, the basic residues (>50%) often occur in tandem or alternating with alanine. In 2003, the structure of a MARCKS peptide bound to calmodulin was solved by crystallography, demonstrating rather surprisingly that the structural interaction was quite similar to that observed for previous CaM kinase peptide complexes (employing 1-10 or 1-14 motifs).
  • There are many other sequences that defy classification based on lack of information or lack of sequence homology to other known calmodulin binding motifs (classified here as "Other" motifs). Some of these sequences may in future be shown to employ already-identified motifs.
  • Sequences in this broad "Others" motif class (including the 1-12 and basic subclasses) have been shown to bind calmodulin primarily in the presence of calcium.

Data

Averages and Links to Graphs

Sequence Alignment, Data and Homologs

1-12
Basic
Others