| Autor: |
Kouno, Takahide, Watanabe, Nobuhisa, Sakai, Naoki, Nakamura, Takashi, Nabeshima, Yuko, Morita, Masashi, Mizuguchi, Mineyuki, Aizawa, Tomoyasu, Demura, Makoto, Imanaka, Tsuneo, Tanaka, Isao, Kawano, Keiichi |
| Jazyk: |
angličtina |
| Rok vydání: |
2011 |
| Předmět: |
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| Zdroj: |
Journal of Molecular Biology. 405(2):560-569 |
| ISSN: |
0022-2836 |
| Popis: |
Physarum polycephalum hemagglutinin I is a 104-residue protein that is secreted to extracellular space. The crystal structure of hemagglutinin I has a β-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the β-sandwich of hemagglutinin I lacks a jelly roll motif and is essentially composed of two simple up-and-down β-sheets. This up-and-down β-sheet motif is well conserved in other lectins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down β-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that hemagglutinin I lacking a jelly roll motif also binds to its target glycopeptide. Taken together, the up-and-down β-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of hemagglutinin I suggests a minimal carbohydrate recognition domain. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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