The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease.

Content Provider	Europe PMC
Author	Babu, M. Madan
Copyright Year	2016
Abstract	In the 1960s, Christian Anfinsen postulated that the unique three-dimensional structure of a protein is determined by its amino acid sequence. This work laid the foundation for the sequence–structure–function paradigm, which states that the sequence of a protein determines its structure, and structure determines function. However, a class of polypeptide segments called intrinsically disordered regions does not conform to this postulate. In this review, I will first describe established and emerging ideas about how disordered regions contribute to protein function. I will then discuss molecular principles by which regulatory mechanisms, such as alternative splicing and asymmetric localization of transcripts that encode disordered regions, can increase the functional versatility of proteins. Finally, I will discuss how disordered regions contribute to human disease and the emergence of cellular complexity during organismal evolution.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC5095923&blobtype=pdf
ISSN	03005127
Journal	Biochemical Society Transactions [Biochem Soc Trans]
Volume Number	44
PubMed Central reference number	PMC5095923
Issue Number	5
PubMed reference number	27911701
e-ISSN	14708752
DOI	10.1042/bst20160172
Language	English
Publisher	Portland Press Ltd.
Publisher Date	2016-10-01
Access Restriction	Open
Rights License	This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY). © 2016 The Author(s)
Subject Keyword	alternative splicing biological networks gene expression and regulation intrinsically disordered proteins protein turnover RNA localization
Content Type	Text
Resource Type	Article
Subject	Biochemistry