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Protein Regulation by Intrinsically Disordered Regions: A Role for Subdomains in the IDR of the HIV‐1 Rev Protein
Author(s) -
Faust Ofrah,
Grunhaus Dana,
Shimshon Odelia,
Yavin Eylon,
Friedler Assaf
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800192
Subject(s) - intrinsically disordered proteins , function (biology) , protein domain , human immunodeficiency virus (hiv) , protein–protein interaction , chemistry , biophysics , protein structure , domain (mathematical analysis) , computational biology , microbiology and biotechnology , biology , biochemistry , gene , mathematics , immunology , mathematical analysis
Intrinsically disordered regions (IDRs) in proteins are highly abundant, but they are still commonly viewed as long stretches of polar, solvent‐accessible residues. Here we show that the disordered C‐terminal domain (CTD) of HIV‐1 Rev has two subregions that carry out two distinct complementary roles of regulating protein oligomerization and contributing to stability. We propose that this takes place through a delicate balance between charged and hydrophobic residues within the IDR. This means that mutations in this region, as well as the known mutations in the structured region of the protein, can affect protein function. We suggest that IDRs in proteins should be divided into subdomains similarly to structured regions, rather than being viewed as long flexible stretches.