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内在无序在中心蛋白瞬时相互作用中的作用。

Role of intrinsic disorder in transient interactions of hub proteins.

作者信息

Singh Gajinder Pal, Ganapathi Mythily, Dash Debasis

机构信息

Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Delhi, India.

出版信息

Proteins. 2007 Mar 1;66(4):761-5. doi: 10.1002/prot.21281.

Abstract

Hubs in the protein-protein interaction network have been classified as "party" hubs, which are highly correlated in their mRNA expression with their partners while "date" hubs show lesser correlation. In this study, we explored the role of intrinsic disorder in date and party hub interactions. The data reveals that intrinsic disorder is significantly enriched in date hub proteins when compared with party hub proteins. Intrinsic disorder has been largely implicated in transient binding interactions. The disorder to order transition, which occurs during binding interactions in disordered regions, renders the interaction highly reversible while maintaining the high specificity. The enrichment of intrinsic disorder in date hubs may facilitate transient interactions, which might be required for date hubs to interact with different partners at different times.

摘要

蛋白质-蛋白质相互作用网络中的枢纽已被分类为“派对”枢纽,其mRNA表达与其伙伴高度相关,而“约会”枢纽的相关性较低。在本研究中,我们探讨了内在无序在约会和派对枢纽相互作用中的作用。数据显示,与派对枢纽蛋白相比,内在无序在约会枢纽蛋白中显著富集。内在无序在很大程度上与瞬时结合相互作用有关。在无序区域的结合相互作用过程中发生的无序到有序转变,使相互作用高度可逆,同时保持高特异性。约会枢纽中内在无序的富集可能促进瞬时相互作用,这可能是约会枢纽在不同时间与不同伙伴相互作用所必需的。

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