7VZO
crystal structure of Domain 5-6 of filamin C from Scylla paramamosain
Summary for 7VZO
| Entry DOI | 10.2210/pdb7vzo/pdb |
| Descriptor | Filamin C, 1,2-ETHANEDIOL, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | allergen, glycoprotein, myogen |
| Biological source | Scylla paramamosain (Mud crab) |
| Total number of polymer chains | 2 |
| Total formula weight | 43394.52 |
| Authors | |
| Primary citation | He, X.R.,Yang, Y.,Kang, S.,Chen, Y.X.,Zheng, P.Y.,Chen, G.X.,Chen, X.M.,Cao, M.J.,Jin, T.,Liu, G.M. Crystal Structure Analysis and IgE Epitope Mapping of Allergic Predominant Region in Scylla paramamosain Filamin C, Scy p 9. J.Agric.Food Chem., 70:1282-1292, 2022 Cited by PubMed Abstract: Filamin C (FLN c) is a novel allergen in shellfish. In this study, FLN c from was divided into three regions for recombinant expression based on the number of domains and amino acids. Using dot blot and basophil activation tests, the allergic predominant region of FLN c was determined to be 336-531 amino acid positions (named FLN c-M). It was confirmed that by X-ray diffraction, the crystal structure of FLN c-M with immunoglobulin-like folding at a resolution of 1.7 Å was obtained. The monomer was a barrel structure composed of 16 β-strands and 2 α-helices. Three conformational epitopes were predicted, six linear epitopes were verified by serological test, and they were positioned on the crystal structure of FLN c-M. For the first time, the crystal structure of the allergic predominant region of FLN c was determined, and it provided an accurate template for the localization of IgE epitopes. PubMed: 35040643DOI: 10.1021/acs.jafc.1c07922 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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