Tandem domain swapping: determinants of multidomain protein misfolding.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
10 2019
10 2019
Historique:
received:
03
05
2019
accepted:
13
05
2019
pubmed:
2
7
2019
medline:
29
7
2020
entrez:
2
7
2019
Statut:
ppublish
Résumé
Tandem homologous domains in proteins are susceptible to misfolding through the formation of domain swaps, non-native conformations involving the exchange of equivalent structural elements between adjacent domains. Cutting-edge biophysical experiments have recently allowed the observation of tandem domain swapping events at the single molecule level. In addition, computer simulations have shed light into the molecular mechanisms of domain swap formation and serve as the basis for methods to systematically predict them. At present, the number of studies on tandem domain swaps is still small and limited to a few domain folds, but they offer important insights into the folding and evolution of multidomain proteins with applications in the field of protein design.
Identifiants
pubmed: 31260947
pii: S0959-440X(19)30057-0
doi: 10.1016/j.sbi.2019.05.012
pmc: PMC6863430
pii:
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
97-104Subventions
Organisme : NIDDK NIH HHS
ID : ZIA DK075104
Pays : United States
Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier Ltd.. All rights reserved.
Références
Proc Natl Acad Sci U S A. 1973 Mar;70(3):697-701
pubmed: 4351801
Angew Chem Int Ed Engl. 2018 May 14;57(20):5674-5678
pubmed: 29512300
Nat Struct Biol. 1999 Nov;6(11):1025-8
pubmed: 10542093
Nat Commun. 2019 Jan 28;10(1):452
pubmed: 30692525
Nat Struct Biol. 2000 Jul;7(7):580-5
pubmed: 10876245
Structure. 2006 Jan;14(1):5-14
pubmed: 16407060
HFSP J. 2008 Dec;2(6):365-77
pubmed: 19436439
J Mol Biol. 2001 Aug 24;311(4):879-90
pubmed: 11518537
Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13786-91
pubmed: 15361578
Nat Struct Biol. 2002 Nov;9(11):818-22
pubmed: 12368899
Proc Natl Acad Sci U S A. 2013 Jan 29;110(5):1680-5
pubmed: 23319605
Database (Oxford). 2011 Sep 29;2011:bar042
pubmed: 21959866
J Mol Biol. 1998 Apr 10;277(4):985-94
pubmed: 9545386
PLoS Comput Biol. 2012;8(3):e1002445
pubmed: 22496628
J Mol Biol. 2008 Sep 26;382(1):223-35
pubmed: 18588900
Biochemistry. 1999 Jan 12;38(2):549-59
pubmed: 9888794
Curr Opin Struct Biol. 2009 Feb;19(1):39-49
pubmed: 19162470
Nat Commun. 2015 Nov 17;6:8861
pubmed: 26572969
Sci Rep. 2016 Sep 23;6:33872
pubmed: 27659606
Prog Biophys Mol Biol. 2017 Sep;128:113-120
pubmed: 27867057
Cold Spring Harb Perspect Biol. 2020 Feb 3;12(2):
pubmed: 30936117
Protein Sci. 2002 Jun;11(6):1285-99
pubmed: 12021428
J Biol Chem. 2016 Feb 19;291(8):4226-35
pubmed: 26703476
Nature. 2005 Dec 8;438(7069):878-81
pubmed: 16341018
J Am Chem Soc. 2012 Mar 7;134(9):4229-35
pubmed: 22296296
Nucleic Acids Res. 2012 Jul;40(Web Server issue):W232-7
pubmed: 22693212
PLoS One. 2012;7(2):e31791
pubmed: 22359629
Bioinformatics. 2006 Jun 1;22(11):1353-8
pubmed: 16543276
Bioinformatics. 2019 Jul 15;35(14):2507-2508
pubmed: 30500878
Adv Exp Med Biol. 2012;747:137-52
pubmed: 22949116
Chem Biol. 2015 Oct 22;22(10):1384-93
pubmed: 26496687
PLoS Comput Biol. 2007 Jun;3(6):e117
pubmed: 17571919
Nat Rev Mol Cell Biol. 2007 Apr;8(4):319-30
pubmed: 17356578
Angew Chem Int Ed Engl. 2010 Dec 17;49(51):9922-5
pubmed: 21104966
PLoS Comput Biol. 2016 May 10;12(5):e1004933
pubmed: 27163669
J Am Chem Soc. 2018 Jul 5;140(26):8096-8099
pubmed: 29923716
Protein Eng. 2001 Aug;14(8):533-42
pubmed: 11579221
Nature. 2011 May 29;474(7353):662-5
pubmed: 21623368
Proc Natl Acad Sci U S A. 2001 May 8;98(10):5596-601
pubmed: 11344301
Nucleic Acids Res. 2009 Jan;37(Database issue):D328-32
pubmed: 18842637
Structure. 2006 May;14(5):811-24
pubmed: 16698543