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Dimer conformation of soluble PECAM-1, an endothelial marker

文献类型： 外文期刊

作者： Jiang, Longguang 1 ; Lin, Lin 3 ; Li, Rui 4 ; Yuan, Cai 2 ; Xu, Mingming 2 ; Huang, Joy H. 5 ; Huang, Mingdong 1 ;

作者机构： 1.Fuzhou Univ, Coll Chem, Fuzhou 350116, Peoples R China

2.Chinese Acad Sci, Fujian Inst Res Struct Matter, State Key Lab Struct Chem, Fuzhou 350002, Peoples R China

3.Harvard Med Sch, Beth Israel Deaconess Med Ctr, Boston, MA 02215 USA

4.Henan Acad Agr Sci, Key Lab Anim Immunol, Minist Agr, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

5.Fudan Univ, Shanghai Med Coll, Shanghai 200032, Peoples R China

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.

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