Structural determinants for Ca2+ and phosphatidylinositol 4,5-bisphosphate binding by the C2A domain of rabphilin-3A.
作者： Nicolas Coudevylle , Pierre Montaville , Andrei Leonov , Markus Zweckstetter , Stefan Becker
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摘要: Rabphilin-3A is a neuronal C2 domain tandem containing protein involved in vesicle trafficking. Both its domains (C2A and C2B) are able to bind phosphatidylinositol 4,5-bisphosphate, key player the neurotransmitter release process. The rabphilin-3A C2A has previously been shown inositol-1,4,5-trisphosphate (IP3; 4,5-bisphosphate headgroup) Ca2+-dependent manner with relatively high affinity (50 microm) presence of saturating concentrations Ca2+. Moreover, IP3 Ca2+ binding mutually enhance each other. Here we present Ca2+-bound solution structure domain. Structural comparison published Ca2+-free crystal revealed that induces conformational change loop 3 (CBL3). Our studies as well our IP3-C2A docking model show active involvement CBL3 binding, suggesting on upon enables interaction vice versa, line target-activated messenger mechanism. data provide detailed structural insight into functional properties reveal for first time determinants
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