Crystallographic Structure of Porcine Adenovirus Type 4 Fiber Head and Galectin Domains
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| Title: | Crystallographic Structure of Porcine Adenovirus Type 4 Fiber Head and Galectin Domains |
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| Authors: | Guardado-Calvo, P., Munoz, E. M., Llamas-Saiz, A. L., Fox, G. C., Kahn, R., Curiel, D. T., Glasgow, D. J. N., van Raaij, M. J. |
| Source: | Digital.CSIC. Repositorio Institucional del CSIC instname Journal of virology 84, 10558-10568 (2010). doi:10.1128/JVI.00997-10 |
| Publisher Information: | American Society for Microbiology, 2010. |
| Publication Year: | 2010 |
| Subject Terms: | Models, Molecular, 0301 basic medicine, Adenoviruses, Porcine: metabolism, Swine, Capsid Proteins: chemistry, Galectins, Genetic Vectors, Molecular Sequence Data, Static Electricity, Adenoviruses, Porcine, Oligosaccharides, Crystallography, X-Ray, Ligands, Adenoviruses, Porcine: classification, 03 medical and health sciences, hexon capsid protein, Adenovirus, Animals, Amino Acid Sequence, Capsid Proteins: metabolism, Oligosaccharides: metabolism, Galectins: metabolism, Galectins: genetics, 0303 health sciences, Binding Sites, Sequence Homology, Amino Acid, Adenoviruses, Porcine: genetics, Oligosaccharides: chemistry, Surface Plasmon Resonance, Protein Structure, Tertiary, 3. Good health, Adenoviruses, Porcine: chemistry, Carbohydrate Sequence, Tandem Repeat Sequences, Capsid Proteins, Galectins: chemistry, Capsid Proteins: genetics |
| Description: | Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N -acetyl-lactosamine units, and we present structures of the galectin domain with lactose, N -acetyl-lactosamine, 3-aminopropyl-lacto- N -neotetraose, and 2-aminoethyl-tri( N -acetyl-lactosamine), confirming the domain as a bona fide galectin domain. |
| Document Type: | Article |
| Language: | English |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.00997-10 |
| Access URL: | https://jvi.asm.org/content/84/20/10558.full.pdf https://pubmed.ncbi.nlm.nih.gov/20686025 http://hdl.handle.net/10261/52235 http://www.rcsb.org/structure/2WSU https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2950603/ http://www.rcsb.org/pdb/explore/explore.do?structureId=2WT0 http://digital.csic.es/bitstream/10261/52235/4/Crystallographic%20structure.pdf https://www.rcsb.org/structure/2WT0 https://www.ncbi.nlm.nih.gov/pubmed/20686025 https://bib-pubdb1.desy.de/record/95000 |
| Rights: | ASM Journals Non-Commercial TDM |
| Accession Number: | edsair.doi.dedup.....f2625f3a9a4216b9499ee927dc5b563c |
| Database: | OpenAIRE |
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Nájsť tento článok vo Web of Science | Abstract: | Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N -acetyl-lactosamine units, and we present structures of the galectin domain with lactose, N -acetyl-lactosamine, 3-aminopropyl-lacto- N -neotetraose, and 2-aminoethyl-tri( N -acetyl-lactosamine), confirming the domain as a bona fide galectin domain. |
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| ISSN: | 10985514 0022538X |
| DOI: | 10.1128/jvi.00997-10 |