| Type: | Domain | Name: | EB1, C-terminal |
| Description: | A group of microtubule-associated proteins called +TIPs (plus end tracking proteins), including EB1 (end-binding protein 1) family proteins, labelgrowing microtubules ends specifically in diverse organisms and are implicated in spindle dynamics, chromosome segregation, and directing microtubules towardcortical sites. EB1 members have a bipartite composition: the N-terminal CHdomain () mediates microtubule plus end localization and a C-terminal cargo binding domain (EB1-C) that captures cell polarity determinants. The EB1-C domain comprises a unique EB1-like sequence motif thatacts as a binding site for other +TIP proteins. It interacts with the carboxy terminus of the adenomatous polyposis coli (APC) tumor suppressor, a wellconserved +TIP phosphoprotein with a pivotal function in cell cycle regulation. Another binding partner of the EB1-C domain is the well conserved+TIP protein dynactin, a component of the large cytoplasmic dynein/dynactin complex [, , ].The ~80-residue EB1-C domain starts with a long smoothly curved helix (alpha1), which is followed by a hairpin connection leading to a short secondhelix (alpha2) running antiparallel to alpha1. The two parallel alpha1 helices of the EB1-C domain dimer wrap around each other in aslightly left-handed supercoil. The two alpha2 helices run antiparallel to helices alpha1 and form a similar fork in the opposite orientation and rotatedby 90 degrees. As a result, two helical segments from each monomer form a four-helix bundle. The side chain forming the hydrophobic core of this bundle are highlyconserved [, , ].Some protein known to contain an EB1-C domain are listed below: Yeast protein BIM1.Fission yeast microtubule integrity protein mal3.Vertebrate microtubule-associated protein RP/EB family member 1 (EB1).Vertebrate microtubule-associated protein RP/EB family member 2 (EB2 or RP1).Vertebrate microtubule-associated protein RP/EB family member 3 (EBF3). | Short Name: | EB1_C |
