Schermatura glicana dei virus di classe I proteine di fusione


Forfatter/Opretter:

Yasunori Watanabe,un b c Thomas A. Bowden,b Ian A. Wilson,d e Max Crispinun

un School of Biological Sciences e Institute of Life Sciences, University of Southampton, Southampton SO17 1BJ, UK

b Divisione di biologia strutturale, Università di Oxford, Wellcome Centre for Human Genetics, Oxford OX3 7BN, Regno Unito

c Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, Regno Unito

d Dipartimento di Biologia Integrativa Strutturale e Computazionale, The Scripps Research Institute, La Jolla, CA 92037, USA

e Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
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Kredit:
Watanabe, Yasunori (2019). "Exploitation of glycosylation in enveloped virus pathobiology". Biochimica et Biophysica Acta (BBA) - General Subjects 1863 (10): 1480–1497. Elsevier BV. DOI:10.1016/j.bbagen.2019.05.012. ISSN 0304-4165.
størrelse:
3573 x 1075 Pixel (902251 Bytes)
beskrivelse:
Glycan Shielding of Viral Class I Fusion Proteins. Left to right: Glycan shield models of Lassa virus GPC (PDB ID: 5VK2) [117,140], Ebola GP (PDB ID: 5JQ3) [141], A/H3N2/361/Victoria/2011 H3N2 Influenza virus hemagglutinin (PDB ID: 4O5N) [142,143], BG505 SOSIP.664 HIV-1 Env (PDB ID: 4ZMJ) [3,144], human coronavirus-NL63 (HCoV-NL63) S protein (PDB ID: 5SZS) [8], Nipah F protein (PDB ID: 5EVM) [145]. Glycans and proteins are shown in blue and grey, respectively. The fusion protein subunit is shown in dark grey. The positions of mucin-like domains of Ebola GP are shown in yellow. Most predominant sugar compositions were modelled onto each N-linked glycan site, using pre-existing GlcNAc residues if possible, with Man5GlcNAc2 modelled on if compositional information was lacking.
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Creative Commons Attribution-Share Alike 4.0

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