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Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt

机译：用DISPROT探索本症蛋白质的手动策划注释

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摘要

DisProt is the major repository of manually curated data for intrinsically disordered proteins collected from the literature. Although lacking a stable tertiary structure under physiological conditions, intrinsically disordered proteins carry out a plethora of biological functions, some of them directly arising from their flexible nature. A growing number of scientific studies have been published during the last few decades in an effort to shed light on their unstructured state, their binding modes,and their functions. DisProt makes use of a team of expert biocurators to provide up‐to‐date annotations of intrinsically disordered proteins from the literature, making them available to the scientific community. Here we present a comprehensive description on how to use DisProt in different contexts and provide a detailed explanation of how to explore and interpret manually curated annotations of intrinsically disordered proteins. We describe how to search DisProt annotations, using both the web interface and the API for programmatic access. Finally, we explain how to visualize and interpret a DisProt entry, p53, a widely studied protein characterized by the presence of unstructured N‐terminal and C‐terminal regions.
机译：Disprot是从文献中收集的本质上无序蛋白质的手动策划数据的主要储存。虽然在生理条件下缺乏稳定的三级结构，但本质上无序的蛋白质进行了一种血清的生物功能，其中一些是它们的灵活性。在过去的几十年中，越来越多的科学研究已经努力在非结构化状态，其装订模式及其功能上阐明光线。 DISPROS利用专家生物调节器团队，提供来自文献的本质上紊乱的蛋白质的最新注释，使其可供科学界提供。在这里，我们提供了关于如何在不同背景下使用DISprot的全面描述，并提供了如何探索和解释本质无序蛋白的手动策划注释的详细说明。我们介绍如何使用Web界面和用于编程访问的API搜索disprott注释。最后，我们解释了如何可视化和解释解压缩条目p53，其特征在于非结构化的n末端和C末端区域的存在。

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