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PDBsum entry 5e1r
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PDB id:
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Allergen
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Title:
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Crystal structure of pecan (carya illinoinensis) vicilin, a new food allergen
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Structure:
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7s vicilin. Chain: a, b, c, d, e, f. Fragment: unp residues 369-792. Engineered: yes
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Source:
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Carya illinoinensis. Pecan. Organism_taxid: 32201. Gene: pec2a1a, pec3a1a, pec4a1a. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.65Å
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R-factor:
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0.219
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R-free:
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0.262
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Authors:
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Y.Z.Zhang
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Key ref:
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Y.Zhang
et al.
(2016).
Identification and Characterization of a New Pecan [Carya illinoinensis (Wangenh.) K. Koch] Allergen, Car i 2.
J Agric Food Chem,
64,
4146-4151.
PubMed id:
DOI:
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Date:
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30-Sep-15
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Release date:
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10-Aug-16
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PROCHECK
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Headers
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References
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B3STU4
(VCL_CARIL) -
Vicilin Car i 2.0101 from Carya illinoinensis
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Seq:
Struc:
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792 a.a.
357 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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J Agric Food Chem
64:4146-4151
(2016)
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PubMed id:
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Identification and Characterization of a New Pecan [Carya illinoinensis (Wangenh.) K. Koch] Allergen, Car i 2.
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Y.Zhang,
B.Lee,
W.X.Du,
S.C.Lyu,
K.C.Nadeau,
L.J.Grauke,
Y.Zhang,
S.Wang,
Y.Fan,
J.Yi,
T.H.McHugh.
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ABSTRACT
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The 7S vicilin and 11S legumin seed storage globulins belong to the cupin
protein superfamily and are major food allergens in many foods from the
"big eight" food allergen groups. Here, for the first time, pecan
vicilin was found to be a food allergen. Western blot experiments revealed that
30% of 27 sera used in this study and 24% of the sera from 25 patients with
double-blind, placebo controlled clinical pecan allergy contained IgE antibodies
specific to pecan vicilin. This allergen consists of a low-complexity region at
its N-terminal and a structured domain at the C-terminal that contains two cupin
motifs and forms homotrimers. The crystal structure of recombinant pecan vicilin
was determined. The refined structure gave R/Rfree values of 0.218/0.262 for all
data to 2.65 Å. There were two trimeric biological units in the
crystallographic asymmetric unit. Pecan vicilin is also a copper protein. These
data may facilitate the understanding of the nutritional value and the
allergenicity relevance of the copper binding property of seed storage proteins
in tree nuts.
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