Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T
Department of Crystallography, Birkbeck College, London, UK.
Nat Struct Biol. 1994 Nov;1(11):782-8. doi: 10.1038/nsb1194-782.
The pleckstrin homology (PH) domain is a conserved module present in many signal transducing and cytoskeletal proteins. Here we report the 2.8 A crystal structure of the PH domain from dynamin. This domain consists of seven beta-strands forming two roughly orthogonal antiparallel beta-sheets terminating with an amphipathic alpha-helix. The structure also reveals a non-covalent dimeric association of the PH domain and a hydrophobic pocket surrounded by a charged rim. The dynamin PH domain structure is discussed in relation to its potential role in mediating interactions between proteins.
普列克底物蛋白同源（PH）结构域是存在于许多信号转导蛋白和细胞骨架蛋白中的保守模块。在此，我们报道了发动蛋白PH结构域的2.8埃晶体结构。该结构域由七条β链组成，形成两个大致正交的反平行β折叠片层，并以一个两亲性α螺旋结束。该结构还揭示了PH结构域的非共价二聚体缔合以及一个由带电荷边缘环绕的疏水口袋。我们结合发动蛋白PH结构域在介导蛋白质间相互作用中的潜在作用对其结构进行了讨论。
