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  • We have identified one lectin that is present on conidia surface of A. fumigatus and thus can be involved in host tissue binding. The binding experiments clearly showed presence of more than one type of binding sites. By preparing protein crystals and solving the 3D structure by X-ray diffraction, we were able to identify six binding sites per monomer. The more complex analysis of structures with different ligands distinguished different binding pattern of each binding site that results in variable specificity and can be correlated with other experimental data.
  • We have identified one lectin that is present on conidia surface of A. fumigatus and thus can be involved in host tissue binding. The binding experiments clearly showed presence of more than one type of binding sites. By preparing protein crystals and solving the 3D structure by X-ray diffraction, we were able to identify six binding sites per monomer. The more complex analysis of structures with different ligands distinguished different binding pattern of each binding site that results in variable specificity and can be correlated with other experimental data. (en)
Title
  • Structural insight into binding variability of Aspergillus fumigatus lectin
  • Structural insight into binding variability of Aspergillus fumigatus lectin (en)
skos:prefLabel
  • Structural insight into binding variability of Aspergillus fumigatus lectin
  • Structural insight into binding variability of Aspergillus fumigatus lectin (en)
skos:notation
  • RIV/00216224:14310/12:00057542!RIV13-GA0-14310___
http://linked.open...avai/riv/aktivita
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  • P(GA303/09/1168), S
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  • 171828
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  • RIV/00216224:14310/12:00057542
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  • lectin; aspergillus; protein structure (en)
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  • [5A6C65E22F9F]
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  • Cioci, Gianluca
  • Houser, Josef
  • Imberty, Anne
  • Komárek, Jan
  • Kostlánová, Nikola
  • Wimmerová, Michaela
http://localhost/t...ganizacniJednotka
  • 14310
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