CAMSAP_CKKMicrotubule-binding calmodulin-regulated spectrin-associated
|SMART accession number:||SM01051|
|Description:||This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.|
|Interpro abstract (IPR014797):|
The CKK domain occurs at the C terminus of a family of proteins collectively defined as calmodulin-regulated spectrin-associated (or CAMSAP) proteins. CAMSAP proteins carry an N-terminal region that includes a CH domain, a central region including a predicted coiled-coil, and this C-terminal CKK domain which is involved in binding CAMSAP proteins to microtubules [(PUBMED:19508979)].
The structure of the CKK domain is a beta-barrel with an associated alpha-helical hairpin. Characteristically, the CKK domain has a single invariant tryptophan residue within the core of the predicted beta-barrel. Residues that interact with this Trp to form part of this core are highly conserved too.
|GO function:||microtubule binding (GO:0008017)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)