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配体结合调节主要桦树花粉过敏原的结构动力学和紧密性。

Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.

作者信息

Grutsch Sarina, Fuchs Julian E, Freier Regina, Kofler Stefan, Bibi Marium, Asam Claudia, Wallner Michael, Ferreira Fátima, Brandstetter Hans, Liedl Klaus R, Tollinger Martin

机构信息

Institute of Organic Chemistry, University of Innsbruck, Innsbruck, Austria.

Institute of General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck, University of Innsbruck, Innsbruck, Austria.

出版信息

Biophys J. 2014 Dec 16;107(12):2972-2981. doi: 10.1016/j.bpj.2014.10.062.

DOI:10.1016/j.bpj.2014.10.062
PMID:25517162
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4269767/
Abstract

Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and transport of small molecules. A prominent member of the PR-10 family, the major birch pollen allergen Bet v 1, is the main cause of spring pollinosis in the temperate climate zone of the northern hemisphere. Bet v 1 binds various ligand molecules to its internal cavity, and immunologic effects of the presence of ligand have been discussed. However, the mechanism of binding has remained elusive. In this study, we show that in solution Bet v 1.0101 is conformationally heterogeneous and cannot be represented by a single structure. NMR relaxation data suggest that structural dynamics are fundamental for ligand access to the protein interior. Complex formation then leads to significant rigidification of the protein along with a compaction of its 3D structure. The data presented herein provide a structural basis for understanding the immunogenic and allergenic potential of ligand binding to Bet v 1 allergens.

摘要

10类病程相关植物蛋白（PR - 10）对于小分子的储存和运输至关重要。PR - 10家族的一个重要成员，主要的桦树花粉过敏原Bet v 1，是北半球温带气候区春季花粉症的主要病因。Bet v 1在其内部腔室结合各种配体分子，并且已经讨论了配体存在的免疫学效应。然而，结合机制仍然难以捉摸。在本研究中，我们表明在溶液中Bet v 1.0101在构象上是异质的，不能由单一结构表示。核磁共振弛豫数据表明结构动力学对于配体进入蛋白质内部至关重要。然后复合物的形成导致蛋白质显著刚性化以及其三维结构的压缩。本文提供的数据为理解配体与Bet v 1过敏原结合的免疫原性和致敏性潜力提供了结构基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/4159cae87b4e/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/d2922a206931/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/ae5caa8cea30/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/e3a669ec3450/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/d580d22dc89b/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/062050fec02c/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/4159cae87b4e/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/d2922a206931/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/ae5caa8cea30/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/e3a669ec3450/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/d580d22dc89b/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/062050fec02c/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2d66/4269767/4159cae87b4e/gr6.jpg

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