Crystal packing analysis of Rhodopsin crystals
Crystal packing analysis of Rhodopsin crystals
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DOI：
10.1016/j.jsb.2007.01.017
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发表时间：
2007-06-01
影响因子：
3
通讯作者：
Stenkamp, Ronald E.
中科院分区：
文献类型：
--
作者：
Lodowski, David T.;Salom, David;Stenkamp, Ronald E.
寡聚化被认为是调节G蛋白偶联受体（GPCR）活性的几种机制之一，但对GPCR寡聚体的结构知之甚少。对视紫红质的两种新晶型的晶体学分析揭示了可能参与功能二聚体或低聚体形成的相互作用表面。新的结晶条件导致形成两种晶体形式，具有类似的视紫红质-视紫红质相互作用，但晶格的变化是由不同的表面活性剂添加剂的加入引起的。然而，在这些晶体结构中的视紫红质分子之间的分子间相互作用可能反映了在视杆外段膜中维持二聚体或低聚体所必需的接触。类似的接触也可以有助于在其他GPCR中形成二聚体或寡聚体。这些新的二聚体与晶体学或EM和AFM研究提出的其他模型进行了比较。每个模型的单体间的表面接触是不同的，但这些模型中的几个一致暗示螺旋I，II，和H-8作为贡献者的主要接触表面稳定的二聚体。(c)2007爱思唯尔公司All rights reserved.
Oligomerization has been proposed as one of several mechanisms to regulate the activity of G protein-coupled receptors (GPCRs), but little is known about the structure of GPCR oligomers. Crystallographic analyses of two new crystal forms of rhodopsin reveal an interaction surface which may be involved in the formation of functional dimers or oligomers. New crystallization conditions lead to the formation of two crystal forms with similar rhodopsin-rhodopsin interactions, but changes in the crystal lattice are induced by the addition of different surfactant additives. However, the intermolecular interactions between rhodopsin molecules in these crystal structures may reflect the contacts necessary for the maintenance of dimers or oligomers in rod outer segment membranes. Similar contacts may assist in the formation of dimers or oligomers in other GPCRs as well. These new dimers are compared with other models proposed by crystallography or EM and AFM studies. The inter-monomer surface contacts are different for each model, but several of these models coincide in implicating helix I, II, and H-8 as contributors to the main contact surface stabilizing the dimers. (c) 2007 Elsevier Inc. All rights reserved.