5xnd

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(New page: '''Unreleased structure''' The entry 5xnd is ON HOLD until Paper Publication Authors: Kumeta, H., Nakayama, H., Ogura, K. Description: Solution structure of the major fish allergen par...)
Current revision (10:31, 14 June 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5xnd is ON HOLD until Paper Publication
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==Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel==
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<StructureSection load='5xnd' size='340' side='right'caption='[[5xnd]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xnd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scomber_japonicus Scomber japonicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XND FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xnd OCA], [https://pdbe.org/5xnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xnd RCSB], [https://www.ebi.ac.uk/pdbsum/5xnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xnd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRVB_SCOJP PRVB_SCOJP] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Kumeta, H., Nakayama, H., Ogura, K.
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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<ref>PMID:29215073</ref>
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Description: Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kumeta, H]]
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<div class="pdbe-citations 5xnd" style="background-color:#fffaf0;"></div>
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[[Category: Ogura, K]]
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[[Category: Nakayama, H]]
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==See Also==
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*[[Parvalbumin|Parvalbumin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Scomber japonicus]]
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[[Category: Kumeta H]]
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[[Category: Nakayama H]]
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[[Category: Ogura K]]

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

PDB ID 5xnd

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