Structure of the MORN4/Myo3a Tail Complex Reveals MORN Repeats as Protein Binding Modules
Structure of the MORN4/Myo3a Tail Complex Reveals MORN Repeats as Protein Binding Modules
复制标题
MORN4/Myo3a 尾部复合物的结构揭示了 MORN 重复序列作为蛋白质结合模块
DOI：
10.1016/j.str.2019.06.004
复制
发表时间：
2019
期刊：
影响因子：
5.7
通讯作者：
Zhang Mingjie
中科院分区：
文献类型：
--
作者：
Li Jianchao;Liu Haiyang;Raval Manmeet H.;Wan Jun;Yengo Christopher M.;Liu Wei;Zhang Mingjie
串联重复序列是构建具有不同结构和功能的蛋白质的基本构件。与广泛研究的基于α螺旋的串联重复序列如锚蛋白、tetratricopeptide、armadillo和HEAT重复序列蛋白相比，对由β发夹形成的串联重复序列蛋白的了解相对较少。在这项研究中，我们发现，MORN重复从MORN 4的功能作为一个蛋白结合模块，特异性地识别来自Myo 3a的尾部货物结合区。MORN 4/Myo 3a复合物的结构显示，MORN 4形成延伸的单层β-折叠结构，并使用U形凹槽以高亲和力和特异性结合Myo 3a尾部。序列和结构分析进一步阐明了MORN重复序列折叠和靶结合的独特序列特征。我们的工作确定了基于β-发夹的MORN重复序列是蛋白质-蛋白质相互作用模块。
Tandem repeats are basic building blocks for constructing proteins with diverse structures and functions. Compared with extensively studied α-helix-based tandem repeats such as ankyrin, tetratricopeptide, armadillo, and HEAT repeat proteins, relatively little is known about tandem repeat proteins formed by β hairpins. In this study, we discovered that the MORN repeats from MORN4 function as a protein binding module specifically recognizing a tail cargo binding region from Myo3a. The structure of the MORN4/Myo3a complex shows that MORN4 forms an extended single-layered β-sheet structure and uses a U-shaped groove to bind to the Myo3a tail with high affinity and specificity. Sequence and structural analyses further elucidated the unique sequence features for folding and target binding of MORN repeats. Our work establishes that the β-hairpin-based MORN repeats are protein-protein interaction modules.