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重新评估重组淋巴细胞受体 NKR-P1A 和 CD69 与化学合成聚糖和肽的结合特性。

Re-evaluation of binding properties of recombinant lymphocyte receptors NKR-P1A and CD69 to chemically synthesized glycans and peptides.

机构信息

Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic.

Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. ^

出版信息

Int J Mol Sci. 2014 Jan 17;15(1):1271-83. doi: 10.3390/ijms15011271.

DOI:10.3390/ijms15011271
PMID:24445261
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3907868/
Abstract

The binding of monosaccharides and short peptides to lymphocyte receptors (human CD69 and rat NKR-P1A) was first reported in 1994 and then in a number of subsequent publications. Based on this observation, numerous potentially high-affinity saccharide ligands have been synthesized over the last two decades in order to utilize their potential in antitumor therapy. Due to significant inconsistencies in their reported binding properties, we decided to re-examine the interaction between multiple ligands and CD69 or NKR-P1A. Using NMR titration and isothermal titration calorimetry we were unable to detect the binding of the tested ligands such as N-acetyl-D-hexosamines and oligopeptides to both receptors, which contradicts the previous observations published in more than twenty papers over the last fifteen years.

摘要

1994 年首次报道了单糖和短肽与淋巴细胞受体(人 CD69 和大鼠 NKR-P1A)的结合,随后在许多后续出版物中也有报道。基于这一观察结果,在过去的二十年中,已经合成了许多具有潜在高亲和力的糖配体,以利用它们在抗肿瘤治疗中的潜力。由于报道的结合特性存在显著差异,我们决定重新检查多种配体与 CD69 或 NKR-P1A 之间的相互作用。使用 NMR 滴定和等温滴定量热法,我们无法检测到测试配体(如 N-乙酰-D-己糖胺和寡肽)与这两种受体的结合,这与过去十五年中二十多篇论文中发表的先前观察结果相矛盾。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/2ba9ec33c19e/ijms-15-01271f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/4322f5dc37df/ijms-15-01271f1a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/3b8c5ac6e91b/ijms-15-01271f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/2ba9ec33c19e/ijms-15-01271f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/4322f5dc37df/ijms-15-01271f1a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/3b8c5ac6e91b/ijms-15-01271f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f6cf/3907868/2ba9ec33c19e/ijms-15-01271f3.jpg

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The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding.激活自然杀伤细胞受体 NKp30 的柄部结构域和糖基化状态对于配体结合很重要。
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4
High-level expression of soluble form of mouse natural killer cell receptor NKR-P1C(B6) in Escherichia coli.小鼠自然杀伤细胞受体NKR-P1C(B6)可溶性形式在大肠杆菌中的高水平表达。
Protein Expr Purif. 2011 Jun;77(2):178-84. doi: 10.1016/j.pep.2011.01.013. Epub 2011 Feb 1.
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