Structure of the pleckstrin homology domain from β-spectrin
Structure of the pleckstrin homology domain from β-spectrin
复制标题
β-血影蛋白的普莱克斯特林同源结构域的结构
作者：
M. Macias;A. Musacchio;H. Ponstingl;M. Nilges;M. Saraste;H. Oschkinat
“普列克底物蛋白同源性”或PH结构域是100个残基的蛋白模块。它存在于许多激酶、磷脂酶C的不同亚型、GTP酶激活蛋白和核苷酸交换因子1 -4中。其功能尚不清楚，但许多含有PH结构域的蛋白质与GTP结合蛋白相互作用5。β-肾上腺素能受体激酶中的PH结构域可能参与与三聚体G蛋白的βγ亚基的结合3，4，6，7。我们在这里报告的三维结构的PH结构域的细胞骨架蛋白血影蛋白使用homeostatic核磁共振。分子的核心是由七条链组成的反平行β折叠。C末端折叠成长α螺旋，另一个螺旋存在于其中一个表面环中。该分子是静电极化的，并且含有可能参与配体结合的口袋。与肽基-脯氨酰-顺反异构酶FKBP有较远的关系，其中该口袋参与大环化合物FK 506的结合（参考文献8-11）。
THE ‘pleckstrin homology’ or PH domain is a 100-residue protein module. It is present in many kinases, different isoforms of phospholipase C, GTPase-activating proteins and nucleotide-exchange factors1–4. Its function is not known, but many proteins that contain a PH domain interact with GTP-binding proteins5. The PH domain in β-adrenergic receptor kinase may be involved in binding to the βγ subunits of a trimeric G-protein3, 4, 6, 7. We report here the three-dimensional structure of the PH domain of the cytoskeletal protein spectrin using homonuclear nuclear magnetic resonance. The core of the molecule is an antiparallel β-sheet consisting of seven strands. The C terminus is folded into a long α-helix, and another helix is present in one of the surface loops. The molecule is electrostatically polarized and contains a pocket which may be involved in the binding of a ligand. There is a distant relationship to the peptidyl-prolyl-cis-trans-isomerase FKBP in which this pocket is involved in the binding of the macrocyclic compound FK506(refs 8–11).
影响因子：
56.9
作者：
THOMAS, JD;SIDERAS, P;PAUL, WE
通讯作者：
PAUL, WE
影响因子：
56.9
作者：
RAWLINGS, DJ;SAFFRAN, DC;WITTE, ON
通讯作者：
WITTE, ON
新型 pleckstrin 同源 (PH) 结构域的鉴定为 PH 结构域功能提供了假设。
影响因子：
3.1
作者：
Shaw,G
通讯作者：
Shaw,G