The constant domain of CRTAM is essential for high-affinity interaction with Nectin-like 2

IF 2.3 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY Biochemistry and Biophysics Reports Pub Date : 2024-08-25 DOI:10.1016/j.bbrep.2024.101813

Juan Carlos Barragan-Galvez , Araceli Hernandez-Flores , Orestes Lopez-Ortega , Adriana A. Rodriguez-Alvarez , Jose Luis Maravillas-Montero , Vianney Ortiz-Navarrete

{"title":"The constant domain of CRTAM is essential for high-affinity interaction with Nectin-like 2","authors":"Juan Carlos Barragan-Galvez , Araceli Hernandez-Flores , Orestes Lopez-Ortega , Adriana A. Rodriguez-Alvarez , Jose Luis Maravillas-Montero , Vianney Ortiz-Navarrete","doi":"10.1016/j.bbrep.2024.101813","DOIUrl":null,"url":null,"abstract":"<div><p>CRTAM (Class-I MHC restricted T cell-associated molecule) is a member of the Nectin-like family, composed of two extracellular domains, one constant domain (IgC) and another variable domain (IgV), expressed in activated CD8 T cells, epithelial cells, natural killer (NK) cells, and in a subpopulation of CD4 T cells. CRTAM recognizes the ligand Nectin-like 2 (Necl2) through the IgV domain. However, the role of the IgC domain during this ligand recognition has yet to be understood. In this study, we show the purification of soluble-folded Ig domains of CRTAM, and we demonstrate that the IgC domain forms a homodimer in solution via hydrophobic interactions. By surface plasmon resonance (SPR) analysis, we also demonstrate that CRTAM binds to Necl2 with an affinity of 2.16 nM. In conclusion, CRTAM's IgC is essential for a high-affinity interaction with Necl-2.</p></div>","PeriodicalId":8771,"journal":{"name":"Biochemistry and Biophysics Reports","volume":"39 ","pages":"Article 101813"},"PeriodicalIF":2.3000,"publicationDate":"2024-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2405580824001778/pdfft?md5=84d08ee3110033c769854fb8a1798734&pid=1-s2.0-S2405580824001778-main.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry and Biophysics Reports","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2405580824001778","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

CRTAM (Class-I MHC restricted T cell-associated molecule) is a member of the Nectin-like family, composed of two extracellular domains, one constant domain (IgC) and another variable domain (IgV), expressed in activated CD8 T cells, epithelial cells, natural killer (NK) cells, and in a subpopulation of CD4 T cells. CRTAM recognizes the ligand Nectin-like 2 (Necl2) through the IgV domain. However, the role of the IgC domain during this ligand recognition has yet to be understood. In this study, we show the purification of soluble-folded Ig domains of CRTAM, and we demonstrate that the IgC domain forms a homodimer in solution via hydrophobic interactions. By surface plasmon resonance (SPR) analysis, we also demonstrate that CRTAM binds to Necl2 with an affinity of 2.16 nM. In conclusion, CRTAM's IgC is essential for a high-affinity interaction with Necl-2.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

CRTAM 的恒定结构域对于与类花蜜蛋白 2 的高亲和性相互作用至关重要

CRTAM（Class-I MHC restricted T cell-associated molecule）是类内毒素家族的成员，由两个胞外结构域组成，一个是恒定结构域（IgC），另一个是可变结构域（IgV），在活化的 CD8 T 细胞、上皮细胞、自然杀伤（NK）细胞和 CD4 T 细胞亚群中表达。CRTAM 通过 IgV 结构域识别配体 Nectin-like 2（Necl2）。然而，IgC 结构域在配体识别过程中的作用尚不清楚。在本研究中，我们纯化了 CRTAM 的可溶性折叠 Ig 结构域，并证明 IgC 结构域在溶液中通过疏水相互作用形成同源二聚体。通过表面等离子共振（SPR）分析，我们还证明了 CRTAM 与 Necl2 的结合亲和力为 2.16 nM。总之，CRTAM 的 IgC 对于与 Necl-2 的高亲和力相互作用至关重要。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Biochemistry and Biophysics Reports Biochemistry, Genetics and Molecular Biology-Biophysics

CiteScore

4.60

自引率

0.00%

发文量

191

审稿时长

59 days

期刊介绍： Open access, online only, peer-reviewed international journal in the Life Sciences, established in 2014 Biochemistry and Biophysics Reports (BB Reports) publishes original research in all aspects of Biochemistry, Biophysics and related areas like Molecular and Cell Biology. BB Reports welcomes solid though more preliminary, descriptive and small scale results if they have the potential to stimulate and/or contribute to future research, leading to new insights or hypothesis. Primary criteria for acceptance is that the work is original, scientifically and technically sound and provides valuable knowledge to life sciences research. We strongly believe all results deserve to be published and documented for the advancement of science. BB Reports specifically appreciates receiving reports on: Negative results, Replication studies, Reanalysis of previous datasets.