The molecular basis for protein kinase A anchoring revealed by solution NMR
The molecular basis for protein kinase A anchoring revealed by solution NMR
复制标题
溶液 NMR 揭示蛋白激酶 A 锚定的分子基础
DOI：
10.1038/6663
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
P. Jennings
中科院分区：
文献类型：
--
作者：
M. G. Newlon;M. Roy;D. Morikis;Z. Hausken;V. Coghlan;John D. Scott;P. Jennings
将信号转导酶区室化为信号复合物是确保细胞内事件特异性的重要机制。这些复合物的形成由参与蛋白质-蛋白质相互作用的专门蛋白质基序介导。腺苷3 ′，5 ′-环磷酸（cAMP）依赖性蛋白激酶（PKA）通过调节（R）亚基二聚体与A-激酶锚定蛋白（AKAP）的相互作用定位。我们现在报告II型PKA R亚基片段RIIα（1-44）的溶液结构，它包括AKAP结合和二聚化界面。该结构包含X型四螺旋束二聚化基序，其具有高亲和力AKAP结合所必需的延伸疏水面。RIIα（1-44）和AKAP片段之间的复合物的NMR数据揭示了两种蛋白质之间的广泛接触。有趣的是，这种相同的二聚化基序也存在于其他信号分子S100家族中。因此，X型四螺旋束可能代表了信号转导中蛋白质-蛋白质相互作用的保守折叠。
Compartmentalization of signal transduction enzymes into signaling complexes is an important mechanism to ensure the specificity of intracellular events. Formation of these complexes is mediated by specialized protein motifs that participate in protein–protein interactions. The adenosine 3´,5´-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) is localized through interaction of the regulatory (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report the solution structure of the type II PKA R-subunit fragment RIIα(1–44), which encompasses both the AKAP-binding and dimerization interfaces. This structure incorporates an X-type four-helix bundle dimerization motif with an extended hydrophobic face that is necessary for high-affinity AKAP binding. NMR data on the complex between RIIα(1–44) and an AKAP fragment reveals extensive contacts between the two proteins. Interestingly, this same dimerization motif is present in other signaling molecules, the S100 family. Therefore, the X-type four-helix bundle may represent a conserved fold for protein–protein interactions in signal transduction.
影响因子：
56.9
作者：
MOCHLYROSEN, D
通讯作者：
MOCHLYROSEN, D
DOI：
10.1073/pnas.94.20.11067
发表时间：
1997-09-30
影响因子：
11.1
作者：
Burton, KA;Johnson, BD;McKnight, GS
通讯作者：
McKnight, GS
影响因子：
56.9
作者：
KNIGHTON, DR;ZHENG, JH;SOWADSKI, JM
通讯作者：
SOWADSKI, JM