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  Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries

Tsai, Y.-X., Chang, N.-E., Reuter, K., Chang, H.-T., Yang, T.-J., von Bülow, S., et al. (2024). Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell, 187(5), 1296-1311. doi:10.1016/j.cell.2024.01.034.

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Tsai, Yu-Xi, Author
Chang, Ning-En, Author
Reuter, Klaus1, Author           
Chang, Hao-Ting, Author
Yang, Tzu-Jing, Author
von Bülow, Sören , Author
Sehrawat, Vidhi, Author
Zerrouki, Noémie, Author
Tuffery, Matthieu, Author
Gecht, Michael, Author
Grothaus, Isabell Louise, Author
Ciacchi, Lucio Colombi, Author
Wang, Yong-Sheng, Author
Hsu, Min-Feng, Author
Khoo, Kay-Hooi, Author
Hummer, Gerhard, Author
Hsu, Shang-Te Danny, Author
Hanus, Cyril, Author
Sikora, Mateusz, Author
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1Max Planck Computing and Data Facility, Max Planck Society, ou_2364734              

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 Abstract: Most membrane proteins are modified by covalent addition of complex sugars through N- and O-glycosylation. Unlike proteins, glycans do not typically adopt specific secondary structures and remain very mobile, shielding potentially large fractions of protein surface. High glycan conformational freedom hinders complete structural elucidation of glycoproteins. Computer simulations may be used to model glycosylated proteins but require hundreds of thousands of computing hours on supercomputers, thus limiting routine use. Here, we describe GlycoSHIELD, a reductionist method that can be implemented on personal computers to graft realistic ensembles of glycan conformers onto static protein structures in minutes. Using molecular dynamics simulation, small-angle X-ray scattering, cryoelectron microscopy, and mass spectrometry, we show that this open-access toolkit provides enhanced models of glycoprotein structures. Focusing on N-cadherin, human coronavirus spike proteins, and gamma-aminobutyric acid receptors, we show that GlycoSHIELD can shed light on the impact of glycans on the conformation and activity of complex glycoproteins.

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 Dates: 2024-02-29
 Publication Status: Published online
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 Identifiers: DOI: 10.1016/j.cell.2024.01.034
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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 187 (5) Sequence Number: - Start / End Page: 1296 - 1311 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183