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ImitateDB:一个包含宿主和病原体蛋白相互作用的结构域和基序模拟的数据库。

ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions.

机构信息

Computational and Structural Biology Laboratory, Department of Biological Sciences and Engineering, Netaji Subhas University of Technology, Dwarka, New Delhi, 110078, India.

Computational and Structural Biology Laboratory, Division of Biotechnology, Netaji Subhas Institute of Technology, Dwarka, New Delhi, 110078, India.

出版信息

Amino Acids. 2022 Jun;54(6):923-934. doi: 10.1007/s00726-022-03163-3. Epub 2022 Apr 30.

Abstract

Molecular mimicry of host proteins by pathogens constitutes a strategy to hijack the host pathways. At present, there is no dedicated resource for mimicked domains and motifs in the host-pathogen interactome. In this work, the experimental host-pathogen (HP) and host-host (HH) protein-protein interactions (PPIs) were collated. The domains and motifs of these proteins were annotated using CD Search and ScanProsite, respectively. Host and pathogen proteins with a shared host interactor and similar domain/motif constitute a mimicry pair exhibiting global structural similarity (domain mimicry pair; DMP) or local sequence motif similarity (motif mimicry pair; MMP). Mimicry pairs are likely to be co-expressed and co-localized. 1,97,607 DMPs and 32,67,568 MMPs were identified in 49,265 experimental HP-PPIs and organized in a web-based resource, ImitateDB ( http://imitatedb.sblab-nsit.net ) that can be easily queried. The results are externally integrated using hyperlinked domain PSSM ID, motif ID, protein ID and PubMed ID. Kinase, UL36, Smc and DEXDc were frequent DMP domains whereas protein kinase C phosphorylation, casein kinase 2 phosphorylation, glycosylation and myristoylation sites were frequent MMP motifs. Novel DMP domains SANT, Tudor, PhoX and MMP motif microbody C-terminal targeting signal, cornichon signature and lipocalin signature were proposed. ImitateDB is a novel resource for identifying mimicry in interacting host and pathogen proteins.

摘要

病原体对宿主蛋白的分子模拟构成了一种劫持宿主途径的策略。目前,在宿主-病原体互作组中还没有专门针对模拟结构域和基序的资源。在这项工作中,我们整理了实验性的宿主-病原体(HP)和宿主-宿主(HH)蛋白-蛋白相互作用(PPIs)。使用 CD Search 和 ScanProsite 分别对这些蛋白质的结构域和基序进行注释。具有共享宿主相互作用蛋白和相似结构域/基序的宿主和病原体蛋白构成了具有全局结构相似性的模拟对(结构域模拟对;DMP)或局部序列基序相似性的模拟对(基序模拟对;MMP)。模拟对可能具有共表达和共定位的特性。在 49265 个实验性 HP-PPI 中,鉴定出 197607 个 DMP 和 3267568 个 MMP,并组织成一个基于网络的资源,ImitateDB(http://imitatedb.sblab-nsit.net),可以轻松查询。使用超链接结构域 PSSM ID、基序 ID、蛋白质 ID 和 PubMed ID 进行外部整合。激酶、UL36、Smc 和 DEXDc 是频繁出现的 DMP 结构域,而蛋白激酶 C 磷酸化、酪蛋白激酶 2 磷酸化、糖基化和豆蔻酰化位点是频繁出现的 MMP 基序。提出了新型 DMP 结构域 SANT、Tudor、PhoX 和 MMP 基序微体 C 末端靶向信号、cornichon 签名和脂联素签名。ImitateDB 是一个用于识别相互作用的宿主和病原体蛋白中模拟结构的新资源。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e808/9054641/8e5262bde103/726_2022_3163_Fig1_HTML.jpg

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