Prediction of the Mannose-Binding Site in the Agaricus bisporus Mannose-Binding Protein.

Autor: Ismaya WT; Dexa Laboratories of Biomolecular Sciences, Industri Selatan V, PP-7, 17550, Cikarang, Indonesia. wangsa.ismaya@dexa-medica.com., Tjandrawinata RR; Dexa Laboratories of Biomolecular Sciences, Industri Selatan V, PP-7, 17550, Cikarang, Indonesia., Rachmawati H; Research Group of Pharmaceutics, School of Pharmacy, Bandung Institute of Technology, Ganesa 10, 40132, Bandung, Indonesia. h_rachmawati@fa.itb.ac.id.; Research Center for Nanosciences and Nanotechnology, Bandung Institute of Technology, Ganesa 10, 40132, Bandung, Indonesia. h_rachmawati@fa.itb.ac.id.
Jazyk: angličtina
Zdroj: The protein journal [Protein J] 2021 Aug; Vol. 40 (4), pp. 554-561. Date of Electronic Publication: 2021 May 06.
DOI: 10.1007/s10930-021-09993-6
Abstrakt: Agaricus bisporus mannose-binding protein (Abmb) was discovered as part of mushroom tyrosinase (PPO3) complex. Apart from its presence, nothing is known about its function or activity in the mushroom. The protein is evolutionarily related to lectins with β-trefoil fold, which are glucose or galactose (and their derivatives) binding proteins. Abmb is also recently showed to display the typical agglutination activity of lectin when in complex with PPO3; this further supports Abmb similarity to its structural homologs from lectin with β-trefoil fold. However, Abmb has no affinity towards glucose or galactose but for mannose, thus its binding to the sugar may be different from its homologs. To date, the natural ligand of Abmb is unknown and the structure of Abmb in the presence of a ligand is not available. Therefore, the mannose-binding site of Abmb was predicted using molecular docking, which was consulted with the information from its structural homologs. This conservative approach would prevent over-speculation. The mannose-binding site of Abmb is likely located in the same region to that of Abmb structural homologs but with a shift in position due to the presence of additional surface loop. In addition, benefiting from the information from an in vitro study on Abmb sugar specificity, the mannose poses suggested that the sugar might interact with the side chains of Arg15, Thr45, Gln48, Asp49, Asp51 and Arg51. Most of these residues were equally present in Abmb structural homologs despite variation of their positions in the amino acid sequence. The variation probably originates from alteration of its amino acid sequence during evolution.
(© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze: MEDLINE
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