5xnd | pdb_00005xnd

Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel

spinqualitylabelsall models 5xnd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xnd is a 1 chain structure with sequence from Scomber japonicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRVB_SCOJP In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity). Publication Abstract from PubMed Although fish is an important part of the human diet, it is also a common source of food allergy. The major allergen in fish is parvalbumin, a well-conserved Ca(2+)-binding protein found in the white muscle of many fish species. Here, we studied the solution structure of the parvalbumin Sco j 1, derived from the Pacific mackerel, using nuclear magnetic resonance spectroscopy. We mapped the IgE-binding epitope proposed in a recent study onto the present structure. Interestingly, three of four residues, which were elucidated as key residues of the IgE-binding epitope, were exposed to solvent, whereas one residue faced the inside of the molecule. We expect that this solution structure can be used in future studies attempting to analyze the various IgE-binding modes of these allergens. Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel.,Kumeta H, Nakayama H, Ogura K Sci Rep. 2017 Dec 7;7(1):17160. doi: 10.1038/s41598-017-17281-6. PMID:29215073 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Parvalbumin

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