The structural and dynamic properties of the cytosolic tails of the adhesion receptor integrin αIIbβ3, fused to a coiled-coil construct via (Gly)₃ linkers, were studied in aqueous solution by nuclear magnetic resonance (NMR) spectroscopy. Both tails were largely flexible and unstructured, although, in the β3 tail, residues Arg⁷²⁴−Ala⁷³⁵ have a propensity to form a helical structure and residues Asn⁷⁴⁴−Tyr⁷⁴⁷ (NPLY) have a propensity to adopt reverse-turn conformations. The mutation β3(Y747A) disrupted this reverse-turn tendency and markedly reduced the affinity of the head domain of the cytoskeletal protein, talin for the β3 tail. Omission of the (Gly)₃ linker connecting the coiled-coiled helices and the integrin tails lead to helix propagation into the β3 tail extending up to eight residues. A variety of different tail constructs were made and studied to reveal tail−tail interactions, but surprisingly no significant interactions between both tails could be detected within the context of our constructs. These results provide structural insight into a highly conserved β tail motif (NPXY/F) required for integrin signaling and highlight a second transiently structured region (residues Arg⁷²⁴−Ala⁷³⁵), which might also be of functional significance.