Dietrich Lars E P, Boeddinghaus Christine, LaGrassa Tracy J, Ungermann Christian
Biochemie Zentrum Heidelberg (BZH), University of Heidelberg, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.
Biochim Biophys Acta. 2003 Aug 18;1641(2-3):111-9. doi: 10.1016/s0167-4889(03)00094-6.
SNARE proteins function at the center of membrane fusion reactions by forming complexes with each other via their coiled-coil domains. Several SNAREs have N-terminal domains (NTDs) that precede the coiled-coil domain and have critical functions in regulating the fusion cascade. This review will highlight recent findings on NTDs of syntaxins, the longin domain of VAMP proteins and SNAP-23/25 homologues in yeast. Biochemical and genetic experiments as well as the resolution of several NMR and crystal structures of SNARE NTDs shed light on their diverse function.
SNARE蛋白通过其卷曲螺旋结构域相互形成复合物，在膜融合反应中发挥核心作用。几种SNARE蛋白具有位于卷曲螺旋结构域之前的N端结构域（NTD），这些结构域在调节融合级联反应中具有关键功能。本综述将重点介绍Syntaxin蛋白NTD、VAMP蛋白的longin结构域以及酵母中SNAP-23/25同源物的最新研究发现。SNARE NTD的生化和遗传学实验以及几种NMR和晶体结构的解析，揭示了它们的多种功能。
