Review
doi: 10.1038/nrm1589.
Intrinsically unstructured proteins and their functions
Affiliations
- PMID: 15738986
- DOI: 10.1038/nrm1589
Item in Clipboard
Review
Intrinsically unstructured proteins and their functions
Nat Rev Mol Cell Biol.
2005 Mar.
Abstract
Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold. Disordered regions can be highly conserved between species in both composition and sequence and, contrary to the traditional view that protein function equates with a stable three-dimensional structure, disordered regions are often functional, in ways that we are only beginning to discover. Many disordered segments fold on binding to their biological targets (coupled folding and binding), whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
Similar articles
-
p53 protein variants: structural and functional similarities with p63 and p73 isoforms.Oncogene. 2004 Jan 22;23(3):631-8. doi: 10.1038/sj.onc.1206929. Oncogene. 2004. PMID: 14737098 Review.
-
Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP.J Mol Biol. 2000 Oct 20;303(2):243-53. doi: 10.1006/jmbi.2000.4141. J Mol Biol. 2000. PMID: 11023789
-
Human homologue of yeast Rad23 protein A interacts with p300/cyclic AMP-responsive element binding (CREB)-binding protein to down-regulate transcriptional activity of p53.Cancer Res. 2001 Jan 1;61(1):64-70. Cancer Res. 2001. PMID: 11196199
-
Transcriptional activator-coactivator recognition: nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding.Biochemistry. 1998 Apr 28;37(17):5858-66. doi: 10.1021/bi9800808. Biochemistry. 1998. PMID: 9558319
-
Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins.Brief Bioinform. 2010 Mar;11(2):225-43. doi: 10.1093/bib/bbp061. Epub 2009 Dec 10. Brief Bioinform. 2010. PMID: 20007729 Review.
Cited by
-
Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation.Front Physiol. 2012 Nov 22;3:435. doi: 10.3389/fphys.2012.00435. eCollection 2012. Front Physiol. 2012. PMID: 23189058 Free PMC article.
-
Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.Proc Natl Acad Sci U S A. 2015 Aug 4;112(31):9614-9. doi: 10.1073/pnas.1512799112. Epub 2015 Jul 20. Proc Natl Acad Sci U S A. 2015. PMID: 26195786 Free PMC article.
-
Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein.Sci Rep. 2020 Aug 7;10(1):13324. doi: 10.1038/s41598-020-70208-6. Sci Rep. 2020. PMID: 32770092 Free PMC article.
-
Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome.PeerJ. 2013 Feb 12;1:e2. doi: 10.7717/peerj.2. Print 2013. PeerJ. 2013. PMID: 23638354 Free PMC article.
-
The Entamoeba histolytica Vps26 (EhVps26) retromeric protein is involved in phagocytosis: Bioinformatic and experimental approaches.PLoS One. 2024 Aug 8;19(8):e0304842. doi: 10.1371/journal.pone.0304842. eCollection 2024. PLoS One. 2024. PMID: 39116045 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
