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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[4ih2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_deliciosa Actinidia deliciosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IH2 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4ih2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_deliciosa Actinidia deliciosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IH2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4igv|4igv]], [[4igw|4igw]], [[4igx|4igx]], [[4igy|4igy]], [[4ih0|4ih0]], [[4ihr|4ihr]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ih2 OCA], [https://pdbe.org/4ih2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ih2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ih2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ih2 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ih2 OCA], [https://pdbe.org/4ih2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ih2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ih2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ih2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KIRO_ACTDE KIRO_ACTDE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Actinidia deliciosa]] | | [[Category: Actinidia deliciosa]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chruszcz, M]] | + | [[Category: Chruszcz M]] |
| - | [[Category: Ciardiello, M A]] | + | [[Category: Ciardiello MA]] |
| - | [[Category: Giangrieco, I]] | + | [[Category: Giangrieco I]] |
| - | [[Category: Minor, W]] | + | [[Category: Minor W]] |
| - | [[Category: Osinski, T]] | + | [[Category: Osinski T]] |
| - | [[Category: Allergen]]
| + | |
| - | [[Category: Mlp/rrp family]]
| + | |
| - | [[Category: Pr-10 related]]
| + | |
| Structural highlights
Function
KIRO_ACTDE
Publication Abstract from PubMed
The allergen Act d 11, also known as kirola, is a 17kDa protein expressed in large amounts in ripe green and yellow-fleshed kiwifruit. Ten percent of all kiwifruit-allergic individuals produce IgE specific for the protein. Using X-ray crystallography, we determined the first three-dimensional structures of Act d 11, produced from both recombinant expression in Escherichia coli and from the natural source (kiwifruit). While Act d 11 is immunologically correlated with the birch pollen allergen Bet v 1 and other members of the pathogenesis-related protein family 10 (PR-10), it has low sequence similarity to PR-10 proteins. By sequence Act d 11 appears instead to belong to the major latex/ripening-related (MLP/RRP) family, but analysis of the crystal structures shows that Act d 11 has a fold very similar to that of Bet v 1 and other PR-10 related allergens regardless of the low sequence identity. The structures of both the natural and recombinant protein include an unidentified ligand, which is relatively small (about 250Da by mass spectrometry experiments) and most likely contains an aromatic ring. The ligand-binding cavity in Act d 11 is also significantly smaller than those in PR-10 proteins. The binding of the ligand, which we were not able to unambiguously identify, results in conformational changes in the protein that may have physiological and immunological implications. Interestingly, the residue corresponding to Glu45 in Bet v 1 (Glu46), which is important for IgE binding to the birch pollen allergen, is conserved in Act d 11, even though it is not in other allergens with significantly higher sequence identity to Bet v 1. We suggest that the so-called Gly-rich loop (or P-loop), which is conserved in all PR-10 allergens, may be responsible for IgE cross-reactivity between Bet v 1 and Act d 11.
Structural and bioinformatic analysis of the kiwifruit allergen Act d 11, a member of the family of ripening-related proteins.,Chruszcz M, Ciardiello MA, Osinski T, Majorek KA, Giangrieco I, Font J, Breiteneder H, Thalassinos K, Minor W Mol Immunol. 2013 Aug 19;56(4):794-803. doi: 10.1016/j.molimm.2013.07.004. PMID:23969108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chruszcz M, Ciardiello MA, Osinski T, Majorek KA, Giangrieco I, Font J, Breiteneder H, Thalassinos K, Minor W. Structural and bioinformatic analysis of the kiwifruit allergen Act d 11, a member of the family of ripening-related proteins. Mol Immunol. 2013 Aug 19;56(4):794-803. doi: 10.1016/j.molimm.2013.07.004. PMID:23969108 doi:10.1016/j.molimm.2013.07.004
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