a heterodimer composed by the TM helices of itsαIIb-andβ3-subunits stabilizes the integrinαIIbβ3 on circulatingplatelets in its resting inactive conformation
In contrasttoαIIbβ3, we found a clear shift in the helical register and peri-odicity of theαvβ3 TM heterodimer such that theαv- andβ3-helices both interacted via small-x3-small residue motifs.
hese resultsconfirm that the conservedβ3S-x3-A-x3-I motif is critical for gatingαvβ3 activation, and that the TM domain surface onβ3usedtobindαv is quite distinct from that used inαIIbβ3
Given the high degree of sequenceconservation in bothα- andβ-chains, it seemed likely that thisTM domain complex might be common to all integrins
the second platelet integrinαvβ3 is instead regu-lated by a distinct TM domain interface, which is also highlyconserved
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