Phafin2 pleckstrin同源结构域的骨干1H, 15N和13C共振分配

IF 0.8 4区生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2021-11-05 DOI:10.1007/s12104-021-10054-3

Jeffrey F. Ellena, Tuo-Xian Tang, Narasimhamurthy Shanaiah, Daniel G. S. Capelluto

{"title":"Phafin2 pleckstrin同源结构域的骨干1H, 15N和13C共振分配","authors":"Jeffrey F. Ellena, Tuo-Xian Tang, Narasimhamurthy Shanaiah, Daniel G. S. Capelluto","doi":"10.1007/s12104-021-10054-3","DOIUrl":null,"url":null,"abstract":"<div><p>Phafin2 is a peripheral protein that triggers cellular signaling from endosomal and lysosomal compartments. The specific subcellular localization of Phafin2 is mediated by the presence of a tandem of phosphatidylinositol 3-phosphate (PtdIns3P)-binding domains, the pleckstrin homology (PH) and the Fab-1, YOTB, Vac1, and EEA1 (FYVE) domains. The requirement for both domains for binding to PtdIns3P still remains unclear. To understand the molecular interactions of the Phafin2 PH domain in detail, we report its nearly complete <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C backbone resonance assignments.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"16 1","pages":"27 - 30"},"PeriodicalIF":0.8000,"publicationDate":"2021-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-021-10054-3.pdf","citationCount":"1","resultStr":"{\"title\":\"Backbone 1H, 15N, and 13C resonance assignments of the Phafin2 pleckstrin homology domain\",\"authors\":\"Jeffrey F. Ellena, Tuo-Xian Tang, Narasimhamurthy Shanaiah, Daniel G. S. Capelluto\",\"doi\":\"10.1007/s12104-021-10054-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Phafin2 is a peripheral protein that triggers cellular signaling from endosomal and lysosomal compartments. The specific subcellular localization of Phafin2 is mediated by the presence of a tandem of phosphatidylinositol 3-phosphate (PtdIns3P)-binding domains, the pleckstrin homology (PH) and the Fab-1, YOTB, Vac1, and EEA1 (FYVE) domains. The requirement for both domains for binding to PtdIns3P still remains unclear. To understand the molecular interactions of the Phafin2 PH domain in detail, we report its nearly complete <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C backbone resonance assignments.</p></div>\",\"PeriodicalId\":492,\"journal\":{\"name\":\"Biomolecular NMR Assignments\",\"volume\":\"16 1\",\"pages\":\"27 - 30\"},\"PeriodicalIF\":0.8000,\"publicationDate\":\"2021-11-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://link.springer.com/content/pdf/10.1007/s12104-021-10054-3.pdf\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomolecular NMR Assignments\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s12104-021-10054-3\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomolecular NMR Assignments","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s12104-021-10054-3","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}

引用次数: 1

摘要

Phafin2是一种外周蛋白，可触发内体和溶酶体间室的细胞信号。Phafin2的特异性亚细胞定位是通过一系列磷脂酰肌醇3-磷酸(PtdIns3P)结合域、pleckstrin同源性(PH)和Fab-1、YOTB、Vac1和EEA1 (FYVE)结构域的存在介导的。绑定到PtdIns3P的两个域的需求仍然不清楚。为了详细了解Phafin2 PH结构域的分子相互作用，我们报告了其几乎完整的1H, 15N和13C骨干共振分配。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

Backbone 1H, 15N, and 13C resonance assignments of the Phafin2 pleckstrin homology domain

Phafin2 is a peripheral protein that triggers cellular signaling from endosomal and lysosomal compartments. The specific subcellular localization of Phafin2 is mediated by the presence of a tandem of phosphatidylinositol 3-phosphate (PtdIns3P)-binding domains, the pleckstrin homology (PH) and the Fab-1, YOTB, Vac1, and EEA1 (FYVE) domains. The requirement for both domains for binding to PtdIns3P still remains unclear. To understand the molecular interactions of the Phafin2 PH domain in detail, we report its nearly complete ¹H, ¹⁵N, and ¹³C backbone resonance assignments.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.