Crystal Structures of the Single PDZ Domains from GRASP65 and their Interaction with the Golgin GM130

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
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引用次数: 4

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