|
The
sequences are divided into motifs based on the distance
between key hydrophobic residues (e.g. Rhoads
and Friedberg, 1997). Numerous structural analyses show
that the key interaction occurs through bulky hydrophobic
residues such as Phe, Trp, Ile, Leu, or Val.
The
1-14 motif
refers to a group of sequences whose key bulky residues are
spaced 12 residues apart. These sequences should be similar
to the characterized binding motifs of smooth muscle and skeletal
muscle myosin light chain kinase (smMLCK, skMLCK) in binding
properties.
The
1-10 motif
refers to a group of sequences whose key bulky residues are
spaced 8 residues apart. They should theoretically be similar
to Ca2+/calmodulin dependent kinase II (CaMKII) in binding properties.
The
1-16 motif
refers to a group of sequences whose key bulky residues are
spaced 14 residues apart. Currently, this motif is believed to
be unique to Ca2+/calmodulin dependent protein kinase kinase (CaMKK).
The
IQ motif
refers to a group of sequences that share the IQ motif found
in a number of mostly Ca2+-independent CaM binding proteins. IQ
motifs have been characterized in several myosins and calcium
channels, such as the L-type calcium channel (Zuhlke
et al., 1999).
The
others class
contains sequences that do not conform to any of the above groups. This may
be due to lack of detailed information describing the molecular interaction between
calmodulin and target.
Please
note that in order to view the database, your browser must
be enabled to run JavaScript and accept cookies.
|
