Energetic pathway sampling in a protein interaction domain

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Energetic pathway sampling in a protein interaction domain. / Hultqvist, Greta; Haq, S. Raza; Punekar, Avinash S.; Chi, Celestine N.; Engström, Ake; Bach, Anders; Strømgaard, Kristian; Selmer, Maria; Gianni, Stefano; Jemth, Per.

In: Structure, Vol. 21, No. 7, 25.06.2013, p. 1193-1202.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hultqvist, G, Haq, SR, Punekar, AS, Chi, CN, Engström, A, Bach, A, Strømgaard, K, Selmer, M, Gianni, S & Jemth, P 2013, 'Energetic pathway sampling in a protein interaction domain', Structure, vol. 21, no. 7, pp. 1193-1202. https://doi.org/10.1016/j.str.2013.05.010

APA

Hultqvist, G., Haq, S. R., Punekar, A. S., Chi, C. N., Engström, A., Bach, A., Strømgaard, K., Selmer, M., Gianni, S., & Jemth, P. (2013). Energetic pathway sampling in a protein interaction domain. Structure, 21(7), 1193-1202. https://doi.org/10.1016/j.str.2013.05.010

Vancouver

Hultqvist G, Haq SR, Punekar AS, Chi CN, Engström A, Bach A et al. Energetic pathway sampling in a protein interaction domain. Structure. 2013 Jun 25;21(7):1193-1202. https://doi.org/10.1016/j.str.2013.05.010

Author

Hultqvist, Greta ; Haq, S. Raza ; Punekar, Avinash S. ; Chi, Celestine N. ; Engström, Ake ; Bach, Anders ; Strømgaard, Kristian ; Selmer, Maria ; Gianni, Stefano ; Jemth, Per. / Energetic pathway sampling in a protein interaction domain. In: Structure. 2013 ; Vol. 21, No. 7. pp. 1193-1202.

Bibtex

@article{99616b8fba1f4842b9fa443dbad485dc,

title = "Energetic pathway sampling in a protein interaction domain",

abstract = "The affinity and specificity of protein-ligand interactions are influenced by energetic crosstalk within the protein domain. However, the molecular details of such intradomain allostery are still unclear. Here, we have experimentally detected and computationally predicted interaction pathways in the postsynaptic density 95/discs large/zonula occludens 1 (PDZ)-peptide ligand model system using wild-type and circularly permuted PDZ proteins. The circular permutant introduced small perturbations in the tertiary structure and a concomitant rewiring of allosteric pathways, allowing us to describe how subtle changes may reshape energetic signaling. The results were analyzed in the context of other members of the PDZ family, which were found to contain distinct interaction pathways for different peptide ligands. The data reveal a fascinating scenario whereby several energetic pathways are sampled within one single domain and distinct pathways are activated by specific protein ligands.",

author = "Greta Hultqvist and Haq, {S. Raza} and Punekar, {Avinash S.} and Chi, {Celestine N.} and Ake Engstr{\"o}m and Anders Bach and Kristian Str{\o}mgaard and Maria Selmer and Stefano Gianni and Per Jemth",

year = "2013",

month = jun,

day = "25",

doi = "10.1016/j.str.2013.05.010",

language = "English",

volume = "21",

pages = "1193--1202",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "7",

}

RIS

TY - JOUR

T1 - Energetic pathway sampling in a protein interaction domain

AU - Hultqvist, Greta

AU - Haq, S. Raza

AU - Punekar, Avinash S.

AU - Chi, Celestine N.

AU - Engström, Ake

AU - Bach, Anders

AU - Strømgaard, Kristian

AU - Selmer, Maria

AU - Gianni, Stefano

AU - Jemth, Per

PY - 2013/6/25

Y1 - 2013/6/25

N2 - The affinity and specificity of protein-ligand interactions are influenced by energetic crosstalk within the protein domain. However, the molecular details of such intradomain allostery are still unclear. Here, we have experimentally detected and computationally predicted interaction pathways in the postsynaptic density 95/discs large/zonula occludens 1 (PDZ)-peptide ligand model system using wild-type and circularly permuted PDZ proteins. The circular permutant introduced small perturbations in the tertiary structure and a concomitant rewiring of allosteric pathways, allowing us to describe how subtle changes may reshape energetic signaling. The results were analyzed in the context of other members of the PDZ family, which were found to contain distinct interaction pathways for different peptide ligands. The data reveal a fascinating scenario whereby several energetic pathways are sampled within one single domain and distinct pathways are activated by specific protein ligands.

AB - The affinity and specificity of protein-ligand interactions are influenced by energetic crosstalk within the protein domain. However, the molecular details of such intradomain allostery are still unclear. Here, we have experimentally detected and computationally predicted interaction pathways in the postsynaptic density 95/discs large/zonula occludens 1 (PDZ)-peptide ligand model system using wild-type and circularly permuted PDZ proteins. The circular permutant introduced small perturbations in the tertiary structure and a concomitant rewiring of allosteric pathways, allowing us to describe how subtle changes may reshape energetic signaling. The results were analyzed in the context of other members of the PDZ family, which were found to contain distinct interaction pathways for different peptide ligands. The data reveal a fascinating scenario whereby several energetic pathways are sampled within one single domain and distinct pathways are activated by specific protein ligands.

U2 - 10.1016/j.str.2013.05.010

DO - 10.1016/j.str.2013.05.010

M3 - Journal article

C2 - 23810696

VL - 21

SP - 1193

EP - 1202

JO - Structure

JF - Structure

SN - 0969-2126

IS - 7

ER -

ID: 49468308