Non-carbohydrate binding partners/domains of animal lectins |
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| Institution: | 1. Department of Agricultural Biotechnology and Research Institute of Agriculture and Life Sciences, College of Agriculture and Life Sciences, Seoul National University, 1 Gwanak–ro, Gwanak–gu, Seoul 08826, Republic of Korea;2. Institute of Green Bio Science and Technology, Pyeongchang 25354, Republic of Korea;1. Applied Electrochemistry, School of Chemical Science and Engineering, KTH Royal Institute of Technology, SE-100 44 Stockholm, Sweden;2. Department of Energy Conversion and Storage, Technical University of Denmark, DK-4000 Roskilde, Denmark;3. SUNCAT Center for Interface Science and Catalysis, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, USA;4. Department of Physics, AlbaNova University Center, Stockholm University, S-106 91 Stockholm, Sweden;1. Key Laboratory of Biology and Genetic Improvement of Horticultural Crops (Northeast Region), Ministry of Agriculture and Rural Affairs/Northeast Agricultural University, Harbin, 150030, China;2. College of Horticulture and Landscape Architecture, Northeast Agricultural University, Harbin, 150030, China;3. Vegetable Research Institute, Guangdong Academy of Agricultural Sciences, Guangzhou, 510640, China;1. Texas A&M AgriLife Research, 11708 Highway 70 South, Vernon, TX, 76384, USA;2. Texas A&M AgriLife Extension, 11708 Highway 70 South, Vernon, TX, 76384, USA |
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| Abstract: | - 1.1. Protein-carbohydrate interactions are involved in a large number of biologically important recognition processes.
- 2.2. Among the participating classes of proteins lectins are defined as carbohydrate-binding proteins other than an antibody or an enzyme.
- 3.3. In addition to the essential carbohydrate-binding domain other functionally and/or structurally important sites, defined by sequence comparison or by experimental demonstration of protein-protein interactions, can be present within the lectin molecule and may be relevant for its physiological significance.
- 4.4. Sequence motifs of lectins for protein-protein interactions include amino acid structures designed for cell adhesion, growth regulatory biosignalling, intracellular routing and enzymatic activity.
- 5.5. Elucidation of the complete functional role(s) of a lectin requires accurate delineation of its carbohydrate and, if present, of its protein ligands.
- 6.6. Presence of more than one carbohydrate-binding domain in a single lectin, potential ligand properties of the glycopart of a lectin, regulatory interplay between different sites and possible interaction of complementarily shaped peptide sequences to the sugar-recognizing site should all be assessed in the quest to comprehensively explain the physiological role(s) of a lectin.
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