TY - JOUR
T1 - A lectin from the Chinese bird-hunting spider binds sialic acids
AU - Siebert, Hans Christian
AU - Lu, Shan Yun
AU - Wechselberger, Rainer
AU - Born, Karin
AU - Eckert, Thomas
AU - Liang, Songping
AU - von der Lieth, Claus Wilhelm
AU - Jiménez-Barbero, Jesús
AU - Schauer, Roland
AU - Vliegenthart, Johannes F G
AU - Lütteke, Thomas
AU - Kožár, Tibor
PY - 2009/8/17
Y1 - 2009/8/17
N2 - 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.
AB - 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.
KW - Carbohydrate-protein interaction
KW - Lectin
KW - Molecular modeling
KW - NMR analysis
KW - Sialic acid
UR - http://www.scopus.com/inward/record.url?scp=68249084780&partnerID=8YFLogxK
U2 - 10.1016/j.carres.2009.06.002
DO - 10.1016/j.carres.2009.06.002
M3 - Article
C2 - 19576577
AN - SCOPUS:68249084780
SN - 0008-6215
VL - 344
SP - 1515
EP - 1525
JO - Carbohydrate Research
JF - Carbohydrate Research
IS - 12
ER -