MembraneinducedalterationsofstructureandsignaltransductionmechanisminthePIP3-bindingdomains

用固体核磁共振、圆二色谱(CD)和荧光光谱研究了Pleckstrin Homology(PH)结构域在溶液和膜表面的构象。PH结构域是已知的调节宿主蛋白膜结合的最大结构域家族之一。信号转导蛋白SWAP-70的膜结合PH结构域发生了剧烈的构象变化，包括二级结构的转变。在膜表面诱导的构象变化被认为是调节SWAP-70的功能，例如响应细胞信号的细胞内重新定位。

Conformations of the pleckstrin homology (PH) domain in solutionand at the membrane surface were examined by using solid-state NMR, circular dichroism(CD) and fluorescence spectroscopy. The PH domains form one of the largest domainfamilies known to regulate membrane association of host proteins. Drastic conformationalalterations including a transition of the secondary structure were detected for themembrane-bound PH domain of a signal transduction protein SWAP-70. Theseconformational alterations induced at the membrane surface are suggested to regulatefunctions of SWAP-70, such as intracellular relocalization in response to the cellularsignaling.