期刊
CARBOHYDRATE POLYMERS
卷 286, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.carbpol.2022.119276
关键词
Linear beta-(1 -> 3)-glucan; Dectin-1; Recognition mode; Molecular dynamic simulation
资金
- Key Research Program of Frontier Sciences, CAS [QYZDY-SSWSLH027]
- National Natural Science Foundation of China [21674114, 91956127, 21604086, 22073093]
- Special Program for Applied Research on Super Computation of the NSFC-Guangdong Joint Fund [U1501501]
Through MD simulation and docking techniques, we investigated the recognition mechanism between bglc and Dectin-1, revealing the important roles of Trp221, His223, and Tyr228 in stabilizing the recognition complex and the clear preference of the recognition mode on the relative direction of triple-helix bglc.
By combining molecular dynamic (MD) simulation and docking techniques, we systematically investigated the recognition between linear beta-(1 -> 3)-glucan (bglc) and Dectin-1. The binding structure exhibits apparent endo- type recognition between the C-type lectin-like domain (CTLD) groove formed by Trp221, His223, Tyr228, as well as other residues around them, and the conformational patterns of triple-helix bglc. Trp221, His223, and Tyr228 play an important role in stabilizing the recognition complex through forming a simple but fixed hydrogen bond network with the C-6 and C-4 hydroxyls. This recognition mode shows a clear preference on the relative direction of the triple-helix bglc with respect to the CTLD groove. Moreover, this recognition mode is not influenced by chain length, except when reaching the lower limit that may destabilize triple-helix formation. Double-helix and single-helix structures lead to unstable recognition, because they abandon the ordered packing pattern in triple-helix and present more flexible chain conformations.
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