Dimer conformation of soluble PECAM-1, an endothelial marker

文献类型： 外文期刊

第一作者： Jiang, Longguang

作者： Jiang, Longguang;Huang, Mingdong;Jiang, Longguang;Yuan, Cai;Xu, Mingming;Huang, Mingdong;Lin, Lin;Li, Rui;Huang, Joy H.

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关键词： PECAM-1;Immunoglobulin domains;Dimer;Homophilic interactions;SAXS

期刊名称：INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY （ 影响因子：5.085； 五年影响因子：4.407 ）

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收录情况： SCI

摘要： Platelet endothelial cell adhesion molecule 1 (PECAM-1) is a cell surface receptor widely distributed on endothelium and hematopoietic-derived cells, and maintain the integrity of the blood vessels. PECAM-1 is widely recognized as an endothelial cell marker. The homophilic interaction through its extracellular domain of PECAM-1 (soluble PECAM-1, or sPECAM-1) is important to its functions. However, structural details for such dimerization are not fully understood. Here we report the production of recombinant sPECAM-1 in large quantity by Drosophila expression system and the small-angle X-ray diffraction (SAXS) study. The recombinant sPECAM-1 was found to form one population of dimer, but not oligomer, and was able to bind to heparin immobilized on a chip in surface plasmon resonance imaging (SPRi) binding experiments. The results of SAXS demonstrated that sPECAM-1 formed a symmetric homodimer of Omega-shape in solution, and each protomer adopted an extended conformation. The dimer is mediated through the intermolecular interactions through the first N-terminal domain (D1) of sPECAM-1. This model provides new structural information for its homophilic interaction mechanism. (C) 2016 Elsevier Ltd. All rights reserved.

分类号： Q5

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