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Structural study of a small molecule receptor bound to dimethyllysine in lysozyme

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Standard

Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. / McGovern, Róise E.; Snarr, Brendan D.; Lyons, Joseph A. et al.
I: Chemical Science, Bind 6, Nr. 1, 01.01.2015, s. 442-449.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

McGovern, RE, Snarr, BD, Lyons, JA, McFarlane, J, Whiting, AL, Paci, I, Hof, F & Crowley, PB 2015, 'Structural study of a small molecule receptor bound to dimethyllysine in lysozyme', Chemical Science, bind 6, nr. 1, s. 442-449. https://doi.org/10.1039/c4sc02383h

APA

McGovern, R. E., Snarr, B. D., Lyons, J. A., McFarlane, J., Whiting, A. L., Paci, I., Hof, F., & Crowley, P. B. (2015). Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. Chemical Science, 6(1), 442-449. https://doi.org/10.1039/c4sc02383h

CBE

McGovern RE, Snarr BD, Lyons JA, McFarlane J, Whiting AL, Paci I, Hof F, Crowley PB. 2015. Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. Chemical Science. 6(1):442-449. https://doi.org/10.1039/c4sc02383h

MLA

Vancouver

McGovern RE, Snarr BD, Lyons JA, McFarlane J, Whiting AL, Paci I et al. Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. Chemical Science. 2015 jan. 1;6(1):442-449. doi: 10.1039/c4sc02383h

Author

McGovern, Róise E. ; Snarr, Brendan D. ; Lyons, Joseph A. et al. / Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. I: Chemical Science. 2015 ; Bind 6, Nr. 1. s. 442-449.

Bibtex

@article{5a1fa003119845aeb75ad829c57d7c7b,
title = "Structural study of a small molecule receptor bound to dimethyllysine in lysozyme",
abstract = "Lysine is a ubiquitous residue on protein surfaces. Post translational modifications of lysine, including methylation to the mono-, di- or trimethylated amine result in chemical and structural alterations that have major consequences for protein interactions and signalling pathways. Small molecules that bind to methylated lysines are potential tools to modify such pathways. To make progress in this direction, detailed structural data of ligands in complex with methylated lysine is required. Here, we report a crystal structure of p-sulfonatocalix[4]arene (sclx4) bound to methylated lysozyme in which the lysine residues were chemically modified from Lys-NH3+ to Lys-NH(Me2)+. Of the six possible dimethyllysine sites, sclx4 selected Lys116-Me2 and the dimethylamino substituent was deeply buried in the calixarene cavity. This complex confirms the tendency for Lys-Me2 residues to form cation-π interactions, which have been shown to be important in protein recognition of histone tails bearing methylated lysines. Supporting data from NMR spectroscopy and MD simulations confirm the selectivity for Lys116-Me2 in solution. The structure presented here may serve as a stepping stone to the development of new biochemical reagents that target methylated lysines. This journal is",
author = "McGovern, {R{\'o}ise E.} and Snarr, {Brendan D.} and Lyons, {Joseph A.} and James McFarlane and Whiting, {Amanda L.} and Irina Paci and Fraser Hof and Crowley, {Peter B.}",
year = "2015",
month = jan,
day = "1",
doi = "10.1039/c4sc02383h",
language = "English",
volume = "6",
pages = "442--449",
journal = "Chemical Science",
issn = "2041-6520",
publisher = "royal society of chemistry",
number = "1",

}

RIS

TY - JOUR

T1 - Structural study of a small molecule receptor bound to dimethyllysine in lysozyme

AU - McGovern, Róise E.

AU - Snarr, Brendan D.

AU - Lyons, Joseph A.

AU - McFarlane, James

AU - Whiting, Amanda L.

AU - Paci, Irina

AU - Hof, Fraser

AU - Crowley, Peter B.

PY - 2015/1/1

Y1 - 2015/1/1

N2 - Lysine is a ubiquitous residue on protein surfaces. Post translational modifications of lysine, including methylation to the mono-, di- or trimethylated amine result in chemical and structural alterations that have major consequences for protein interactions and signalling pathways. Small molecules that bind to methylated lysines are potential tools to modify such pathways. To make progress in this direction, detailed structural data of ligands in complex with methylated lysine is required. Here, we report a crystal structure of p-sulfonatocalix[4]arene (sclx4) bound to methylated lysozyme in which the lysine residues were chemically modified from Lys-NH3+ to Lys-NH(Me2)+. Of the six possible dimethyllysine sites, sclx4 selected Lys116-Me2 and the dimethylamino substituent was deeply buried in the calixarene cavity. This complex confirms the tendency for Lys-Me2 residues to form cation-π interactions, which have been shown to be important in protein recognition of histone tails bearing methylated lysines. Supporting data from NMR spectroscopy and MD simulations confirm the selectivity for Lys116-Me2 in solution. The structure presented here may serve as a stepping stone to the development of new biochemical reagents that target methylated lysines. This journal is

AB - Lysine is a ubiquitous residue on protein surfaces. Post translational modifications of lysine, including methylation to the mono-, di- or trimethylated amine result in chemical and structural alterations that have major consequences for protein interactions and signalling pathways. Small molecules that bind to methylated lysines are potential tools to modify such pathways. To make progress in this direction, detailed structural data of ligands in complex with methylated lysine is required. Here, we report a crystal structure of p-sulfonatocalix[4]arene (sclx4) bound to methylated lysozyme in which the lysine residues were chemically modified from Lys-NH3+ to Lys-NH(Me2)+. Of the six possible dimethyllysine sites, sclx4 selected Lys116-Me2 and the dimethylamino substituent was deeply buried in the calixarene cavity. This complex confirms the tendency for Lys-Me2 residues to form cation-π interactions, which have been shown to be important in protein recognition of histone tails bearing methylated lysines. Supporting data from NMR spectroscopy and MD simulations confirm the selectivity for Lys116-Me2 in solution. The structure presented here may serve as a stepping stone to the development of new biochemical reagents that target methylated lysines. This journal is

UR - http://www.scopus.com/inward/record.url?scp=84915819818&partnerID=8YFLogxK

U2 - 10.1039/c4sc02383h

DO - 10.1039/c4sc02383h

M3 - Journal article

AN - SCOPUS:84915819818

VL - 6

SP - 442

EP - 449

JO - Chemical Science

JF - Chemical Science

SN - 2041-6520

IS - 1

ER -