Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces
文献类型：期刊论文
| 作者 | Chen, Rong1; Qi, Jianxun2; Yuan, Hongyu1; Wu, Yanan1; Hu, Wei3; Xia, Chun1,4 |
| 刊名 | JOURNAL OF STRUCTURAL BIOLOGY
 |
| 出版日期 | 2015-03-01 |
| 卷号 | 189期号:3页码:259-268 |
| 关键词 | Pentraxin Trimer Zebrafish Structure Evolution |
| ISSN号 | 1047-8477 |
| 通讯作者 | Xia, C (reprint author), China Agr Univ, Coll Vet Med, Dept Microbiol & Immunol, Beijing 100094, Peoples R China. |
| 英文摘要 | Short-chain pentraxins (PTXs), including CRP and SAP, are innate pattern recognition receptors that play vital roles in the recognition and elimination of various pathogenic bacteria by triggering the classical complement pathway through C1q. Similar to antibodies, pentraxins can also activate opsonisation and phagocytosis by interacting with Fc receptors (FcRs). Various structural studies on human PTXs have been performed, but there are no reports about the crystal structure of bony fish pentraxins. Here, the crystal structures of zebrafish PTX (Dare-PTX-Ca and Dare-PTX) are presented. Both Dare-PTX-Ca and Dare-PTX are cyclic trimers, which are new forms of crystallised pentraxins. The structures reveal that the ligand-binding pocket (LBP) in the recognition face of Dare-PTX is deep and narrow. Homology modelling shows that LBPs from different Dare-PTX loci differ in shape, reflecting their specific recognition abilities. Furthermore, in comparison with the structure of hCPR, a new C1q binding mode was identified in Dare-PTX. In addition, the FcR-binding sites of hSAP are partially conserved in Dare-PTX. These results will shed light on the understanding of a primitive PTX in bony fish, which evolved approximately 450 million years ago. (C) 2015 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 关键词[WOS] | C-REACTIVE PROTEIN ; AMYLOID-P COMPONENT ; CARP CYPRINUS-CARPIO ; SITE-DIRECTED MUTAGENESIS ; SAP-LIKE PENTRAXIN ; MAXIMUM-LIKELIHOOD ; COMPLEMENT-SYSTEM ; C1Q-BINDING SITE ; LIMULUS SAP ; X-RAY |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000351249500011 |
| 源URL | [http://ir.ihb.ac.cn/handle/342005/23902]  |
| 专题 | 水生生物研究所_鱼类生物学及渔业生物技术研究中心_期刊论文 |
| 作者单位 | 1.China Agr Univ, Coll Vet Med, Dept Microbiol & Immunol, Beijing 100094, Peoples R China 2.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol Immunol CASPMI, Beijing 100101, Peoples R China 3.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China 4.China Agr Univ, Coll Vet Med, Minist Agr, Key Lab Anim Epidemiol & Zoonosis, Beijing 100094, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chen, Rong,Qi, Jianxun,Yuan, Hongyu,et al. Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces[J]. JOURNAL OF STRUCTURAL BIOLOGY,2015,189(3):259-268. |
| APA | Chen, Rong,Qi, Jianxun,Yuan, Hongyu,Wu, Yanan,Hu, Wei,&Xia, Chun.(2015).Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces.JOURNAL OF STRUCTURAL BIOLOGY,189(3),259-268. |
| MLA | Chen, Rong,et al."Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces".JOURNAL OF STRUCTURAL BIOLOGY 189.3(2015):259-268. |
入库方式： OAI收割
来源：水生生物研究所
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