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OTHERS
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- 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.
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