Calmodulin-regulated spectrin-associated CKK domain

In molecular biology, the calmodulin-regulated spectrin-associated CKK domain (also known as the CKK domain) is a domain which occurs at the C-terminus 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. This 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 this domain in murine hypothetical protein has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.[1]

CAMSAP_CKK
solution structure of a murine hypothetical protein from riken cdna 2310057j16
Identifiers
SymbolCAMSAP_CKK
PfamPF08683
Pfam clanCL0350
InterProIPR014797
SCOP21ugj / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References
  1. Baines AJ, Bignone PA, King MD, Maggs AM, Bennett PM, Pinder JC, Phillips GW (September 2009). "The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins". Molecular Biology and Evolution. 26 (9): 2005–14. doi:10.1093/molbev/msp115. PMID 19508979.
This article incorporates text from the public domain Pfam and InterPro: IPR014797
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