GRASP65单PDZ结构域的晶体结构及其和Golgin GM130的相互作用

IF 0.7 4区 化学 Q4 CHEMISTRY, MULTIDISCIPLINARY Croatica Chemica Acta Pub Date : 2019-04-24 DOI:10.5562/CCA3341
C. M. Jurk, Y. Roske, U. Heinemann
{"title":"GRASP65单PDZ结构域的晶体结构及其和Golgin GM130的相互作用","authors":"C. M. Jurk, Y. Roske, U. Heinemann","doi":"10.5562/CCA3341","DOIUrl":null,"url":null,"abstract":"Among the major components of the Golgi apparatus are the GRASP family proteins, including GRASP65 on the cis-Golgi side. With its GRASP domain, GRASP65 is involved in Golgi stacking and ribbon formation. Interaction of GRASP65 with the Golgi marker protein GM130 is important for the docking of vesicles to the Golgi membrane. We present here structures of the two individual PDZ domains comprising the GRASP domain in human GRASP65. We use isothermal titration calorimetry to probe the interaction between GRASP65 and GM130. Additionally, we present evidence for the limited sequence conservation of the PDZ fold by describing the PDZ domain structure of the GRASP65 homolog Grh1 from Saccharomyces cerevisiae.","PeriodicalId":10822,"journal":{"name":"Croatica Chemica Acta","volume":"91 1","pages":"255-264"},"PeriodicalIF":0.7000,"publicationDate":"2019-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":"{\"title\":\"Crystal Structures of the Single PDZ Domains from GRASP65 and their Interaction with the Golgin GM130\",\"authors\":\"C. M. Jurk, Y. Roske, U. Heinemann\",\"doi\":\"10.5562/CCA3341\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Among the major components of the Golgi apparatus are the GRASP family proteins, including GRASP65 on the cis-Golgi side. With its GRASP domain, GRASP65 is involved in Golgi stacking and ribbon formation. Interaction of GRASP65 with the Golgi marker protein GM130 is important for the docking of vesicles to the Golgi membrane. We present here structures of the two individual PDZ domains comprising the GRASP domain in human GRASP65. We use isothermal titration calorimetry to probe the interaction between GRASP65 and GM130. Additionally, we present evidence for the limited sequence conservation of the PDZ fold by describing the PDZ domain structure of the GRASP65 homolog Grh1 from Saccharomyces cerevisiae.\",\"PeriodicalId\":10822,\"journal\":{\"name\":\"Croatica Chemica Acta\",\"volume\":\"91 1\",\"pages\":\"255-264\"},\"PeriodicalIF\":0.7000,\"publicationDate\":\"2019-04-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Croatica Chemica Acta\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.5562/CCA3341\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Croatica Chemica Acta","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.5562/CCA3341","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 4

摘要

高尔基体的主要成分是GRASP家族蛋白,包括顺式高尔基体侧的GRASP65。GRASP65具有GRASP结构域,参与高尔基体堆积和带状体形成。GRASP65与高尔基标记蛋白GM130的相互作用对于囊泡与高尔基膜的对接是重要的。我们在这里展示了包括人类GRASP65中的GRASP结构域的两个单独的PDZ结构域的结构。我们使用等温滴定量热法来探测GRASP65和GM130之间的相互作用。此外,我们通过描述酿酒酵母GRASP65同源物Grh1的PDZ结构域结构,为PDZ折叠的有限序列保守性提供了证据。
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
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Crystal Structures of the Single PDZ Domains from GRASP65 and their Interaction with the Golgin GM130
Among the major components of the Golgi apparatus are the GRASP family proteins, including GRASP65 on the cis-Golgi side. With its GRASP domain, GRASP65 is involved in Golgi stacking and ribbon formation. Interaction of GRASP65 with the Golgi marker protein GM130 is important for the docking of vesicles to the Golgi membrane. We present here structures of the two individual PDZ domains comprising the GRASP domain in human GRASP65. We use isothermal titration calorimetry to probe the interaction between GRASP65 and GM130. Additionally, we present evidence for the limited sequence conservation of the PDZ fold by describing the PDZ domain structure of the GRASP65 homolog Grh1 from Saccharomyces cerevisiae.
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
Croatica Chemica Acta
Croatica Chemica Acta 化学-化学综合
CiteScore
0.60
自引率
0.00%
发文量
3
审稿时长
18 months
期刊介绍: Croatica Chemica Acta (Croat. Chem. Acta, CCA), is an international journal of the Croatian Chemical Society publishing scientific articles of general interest to chemistry.
期刊最新文献
Spectrophotometric Determination of N-acetyl-L-Cysteine in Pharmaceutical Formulations by Flow Injection and Sequential Injection Analysis: Comparison of the Methods Comparison of Radon Adsorption on Hematite and Charcoal Activated Powder in Air Synthesis, Experimental and Theoretical Characterization of (μ4-oxo)hexakis(μ2-chloro)-tetrakis[1-(allyl)-1H-imidazole]tetracopper(II) Ecofriendly Synthesis of DHPMs using Copper-based Nano catalysts and Evaluation of Antibacterial Activity Influence of Bitartrate Ion Concentration in the Copper Electrodeposition Onto a Polycrystalline Gold Electrode
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1