6G47
Crystal Structure of Human Adenovirus 52 Short Fiber Knob in Complex with alpha-(2,8)-Trisialic Acid (DP3)
Summary for 6G47
| Entry DOI | 10.2210/pdb6g47/pdb |
| Related | 4XL8 |
| Descriptor | Fiber-1, N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid, N-acetyl-alpha-neuraminic acid, ... (7 entities in total) |
| Functional Keywords | polysialic acid, adenovirus, virolectin, fiber knob, cell attachment, viral entry, carbohydrate, cell adhesion |
| Biological source | Human adenovirus 52 |
| Total number of polymer chains | 3 |
| Total formula weight | 68767.26 |
| Authors | Liaci, A.M.,Stehle, T. (deposition date: 2018-03-26, release date: 2018-05-02, Last modification date: 2024-01-17) |
| Primary citation | Lenman, A.,Liaci, A.M.,Liu, Y.,Frangsmyr, L.,Frank, M.,Blaum, B.S.,Chai, W.,Podgorski, I.I.,Harrach, B.,Benko, M.,Feizi, T.,Stehle, T.,Arnberg, N. Polysialic acid is a cellular receptor for human adenovirus 52. Proc. Natl. Acad. Sci. U.S.A., 115:E4264-E4273, 2018 Cited by PubMed Abstract: Human adenovirus 52 (HAdV-52) is one of only three known HAdVs equipped with both a long and a short fiber protein. While the long fiber binds to the coxsackie and adenovirus receptor, the function of the short fiber in the virus life cycle is poorly understood. Here, we show, by glycan microarray analysis and cellular studies, that the short fiber knob (SFK) of HAdV-52 recognizes long chains of α-2,8-linked polysialic acid (polySia), a large posttranslational modification of selected carrier proteins, and that HAdV-52 can use polySia as a receptor on target cells. X-ray crystallography, NMR, molecular dynamics simulation, and structure-guided mutagenesis of the SFK reveal that the nonreducing, terminal sialic acid of polySia engages the protein with direct contacts, and that specificity for polySia is achieved through subtle, transient electrostatic interactions with additional sialic acid residues. In this study, we present a previously unrecognized role for polySia as a cellular receptor for a human viral pathogen. Our detailed analysis of the determinants of specificity for this interaction has general implications for protein-carbohydrate interactions, particularly concerning highly charged glycan structures, and provides interesting dimensions on the biology and evolution of members of . PubMed: 29674446DOI: 10.1073/pnas.1716900115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.497 Å) |
Structure validation
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