| Primary Identifier | IPR014797 | Type | Domain |
| Short Name | CKK_CAMSAP |
| description | The CKK domain occurs at the C-terminal in CAMSAP proteins. The structure of the CKK domain is a ��-barrel with an associated ��-helical hairpin. Characteristically, the CKK domain has a single invariant tryptophan residue within the core of the predicted ��-barrel. Residues that interact with this Trp to form part of this core are highly conserved too.The calmodulin-regulated spectrin-associated (CAMSAP) proteins are defined by a CKK domain that binds microtubules []. It includes CAMSAPs from vertebrates and Patronin from invertebrates []. CAMSAP1 is the representative member. It contains a conserved region, CC1, that binds to both spectrin and Ca2+/calmodulin in vitro and links spectrin-binding to neurite outgrowth []. Patronin binds to and protects the MT minus-end against depolymerization []. CAMSAP2 is a key microtubule-organising protein that specifically binds the minus end of non-centrosomal microtubules and regulates their dynamics and organisation. CAMSAP proteins carry an N-terminal region that includes two CH domains represented by and , a central region including a predicted coiled-coil, and a C-terminal CKK domain , which is involved in binding CAMSAP proteins to microtubules []. |
