Selectivity determinants of GPCR-G-protein binding

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Standard

Selectivity determinants of GPCR-G-protein binding. / Flock, Tilman; Hauser, Alexander S; Lund, Nadia; Gloriam, David E; Balaji, Santhanam; Babu, M Madan.

I: Nature, Bind 545, Nr. 7654, 18.05.2017, s. 317-322.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Flock, T, Hauser, AS, Lund, N, Gloriam, DE, Balaji, S & Babu, MM 2017, 'Selectivity determinants of GPCR-G-protein binding', Nature, bind 545, nr. 7654, s. 317-322. https://doi.org/10.1038/nature22070

APA

Flock, T., Hauser, A. S., Lund, N., Gloriam, D. E., Balaji, S., & Babu, M. M. (2017). Selectivity determinants of GPCR-G-protein binding. Nature, 545(7654), 317-322. https://doi.org/10.1038/nature22070

Vancouver

Flock T, Hauser AS, Lund N, Gloriam DE, Balaji S, Babu MM. Selectivity determinants of GPCR-G-protein binding. Nature. 2017 maj 18;545(7654):317-322. https://doi.org/10.1038/nature22070

Author

Flock, Tilman ; Hauser, Alexander S ; Lund, Nadia ; Gloriam, David E ; Balaji, Santhanam ; Babu, M Madan. / Selectivity determinants of GPCR-G-protein binding. I: Nature. 2017 ; Bind 545, Nr. 7654. s. 317-322.

Bibtex

@article{f6e5e81f826e4cf09d8e1a5555f49c07,
title = "Selectivity determinants of GPCR-G-protein binding",
abstract = "The selective coupling of G-protein-coupled receptors (GPCRs) to specific G proteins is critical to trigger the appropriate physiological response. However, the determinants of selective binding have remained elusive. Here we reveal the existence of a selectivity barcode (that is, patterns of amino acids) on each of the 16 human G proteins that is recognized by distinct regions on the approximately 800 human receptors. Although universally conserved positions in the barcode allow the receptors to bind and activate G proteins in a similar manner, different receptors recognize the unique positions of the G-protein barcode through distinct residues, like multiple keys (receptors) opening the same lock (G protein) using non-identical cuts. Considering the evolutionary history of GPCRs allows the identification of these selectivity-determining residues. These findings lay the foundation for understanding the molecular basis of coupling selectivity within individual receptors and G proteins.",
keywords = "Amino Acid Sequence, GPCR, Evolution, Molecular, G-protein-coupled receptor, G proteins, Structural Homology, Protein",
author = "Tilman Flock and Hauser, {Alexander S} and Nadia Lund and Gloriam, {David E} and Santhanam Balaji and Babu, {M Madan}",
year = "2017",
month = may,
day = "18",
doi = "10.1038/nature22070",
language = "English",
volume = "545",
pages = "317--322",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",
number = "7654",

}

RIS

TY - JOUR

T1 - Selectivity determinants of GPCR-G-protein binding

AU - Flock, Tilman

AU - Hauser, Alexander S

AU - Lund, Nadia

AU - Gloriam, David E

AU - Balaji, Santhanam

AU - Babu, M Madan

PY - 2017/5/18

Y1 - 2017/5/18

N2 - The selective coupling of G-protein-coupled receptors (GPCRs) to specific G proteins is critical to trigger the appropriate physiological response. However, the determinants of selective binding have remained elusive. Here we reveal the existence of a selectivity barcode (that is, patterns of amino acids) on each of the 16 human G proteins that is recognized by distinct regions on the approximately 800 human receptors. Although universally conserved positions in the barcode allow the receptors to bind and activate G proteins in a similar manner, different receptors recognize the unique positions of the G-protein barcode through distinct residues, like multiple keys (receptors) opening the same lock (G protein) using non-identical cuts. Considering the evolutionary history of GPCRs allows the identification of these selectivity-determining residues. These findings lay the foundation for understanding the molecular basis of coupling selectivity within individual receptors and G proteins.

AB - The selective coupling of G-protein-coupled receptors (GPCRs) to specific G proteins is critical to trigger the appropriate physiological response. However, the determinants of selective binding have remained elusive. Here we reveal the existence of a selectivity barcode (that is, patterns of amino acids) on each of the 16 human G proteins that is recognized by distinct regions on the approximately 800 human receptors. Although universally conserved positions in the barcode allow the receptors to bind and activate G proteins in a similar manner, different receptors recognize the unique positions of the G-protein barcode through distinct residues, like multiple keys (receptors) opening the same lock (G protein) using non-identical cuts. Considering the evolutionary history of GPCRs allows the identification of these selectivity-determining residues. These findings lay the foundation for understanding the molecular basis of coupling selectivity within individual receptors and G proteins.

KW - Amino Acid Sequence

KW - GPCR

KW - Evolution, Molecular

KW - G-protein-coupled receptor

KW - G proteins

KW - Structural Homology, Protein

U2 - 10.1038/nature22070

DO - 10.1038/nature22070

M3 - Journal article

C2 - 28489817

VL - 545

SP - 317

EP - 322

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7654

ER -

ID: 183123626