| Autor: |
Siebert HC; Institut für Biochemie und Endokrinologie, Fachbereich für Veterinärmedizin, Justus-Liebig Universität Giessen, Frankfurter Strasse 100, 35392 Giessen, Germany., Lu SY, Wechselberger R, Born K, Eckert T, Liang S, von der Lieth CW, Jiménez-Barbero J, Schauer R, Vliegenthart JF, Lütteke T, André S, Kaltner H, Gabius HJ, Kozár T |
| Jazyk: |
angličtina |
| Zdroj: |
Carbohydrate research [Carbohydr Res] 2009 Aug 17; Vol. 344 (12), pp. 1515-25. Date of Electronic Publication: 2009 Jun 06. |
| DOI: |
10.1016/j.carres.2009.06.002 |
| Abstrakt: |
The affinity to sialic acid-containing oligosaccharides of the small-animal lectin SHL-I isolated from the venom of the Chinese bird-hunting spider Selenocosmia huwena is here described for the first time. By a strategic combination of NMR techniques, molecular modeling, and data mining tools it was possible to identify the crucial amino acid residues that are responsible for SHL-I's ability to bind sialic acid residues in a specific way. Furthermore, we are able to discuss the role of the functional groups of sialic acid when bound to SHL-I. Also the impact of Pro31 in its cis- or trans-form on SHL-I's ligand affinity is of special interest, since it answers the question if Trp32 is a crucial amino acid for stabilizing complexes between SHL-I and sialic acid. SHL-I can be considered as a proper model system that provides further insights into the binding mechanisms of small-animal lectins to sialic acid on a sub-molecular level. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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