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PDBsum entry 4pph
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Plant protein
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PDB id
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4pph
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References listed in PDB file
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Key reference
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Title
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Structure of γ-Conglutin: insight into the quaternary structure of 7s basic globulins from legumes.
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Authors
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J.Czubinski,
J.Barciszewski,
M.Gilski,
K.Szpotkowski,
J.Debski,
E.Lampart-Szczapa,
M.Jaskolski.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2015,
71,
224-238.
[DOI no: ]
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PubMed id
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Abstract
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γ-Conglutin from lupin seeds is an unusual 7S basic globulin protein. It is
capable of reducing glycaemia in mammals, but the structural basis of this
activity is not known. γ-Conglutin shares a high level of structural homology
with glycoside hydrolase inhibitor proteins, although it lacks any kind of
inhibitory activity against plant cell-wall degradation enzymes. In addition,
γ-conglutin displays a less pronounced structural similarity to pepsin-like
aspartic proteases, but it is proteolytically dysfunctional. Only one structural
study of a legume 7S basic globulin, that isolated from soybean, has been
reported to date. The quaternary assembly of soybean 7S basic globulin (Bg7S) is
arranged as a cruciform-shaped tetramer comprised of two superposed dimers.
Here, the crystal structure of γ-conglutin isolated from Lupinus angustifolius
seeds (LangC) is presented. The polypeptide chain of LangC is
post-translationally cleaved into α and β subunits but retains its covalent
integrity owing to a disulfide bridge. The protomers of LangC undergo an
intricate quaternary assembly, resulting in a ring-like hexamer with
noncrystallographic D3 symmetry. The twofold-related dimers are similar to those
in Bg7S but their assembly is different as a consequence of mutations in a
β-strand that is involved in intermolecular β-sheet formation in γ-conglutin.
Structural elucidation of γ-conglutin will help to explain its physiological
role, especially in the evolutionary context, and will guide further research
into the hypoglycaemic activity of this protein in humans, with potential
consequences for novel antidiabetic therapies.
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Secondary reference #1
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Title
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Characterisation of different digestion susceptibility of lupin seed globulins.
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Authors
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J.Czubinski,
K.Dwiecki,
A.Siger,
G.Neunert,
E.Lampart-Szczapa.
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Ref.
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Food Chem, 2014,
143,
418-426.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Release of flavonoids from lupin globulin proteins during digestion in a model system.
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Authors
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J.Czubinski,
K.Dwiecki,
A.Siger,
P.Kachlicki,
G.Neunert,
E.Lampart-Szczapa,
M.Nogala-Kalucka.
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Ref.
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J Agric Food Chem, 2012,
60,
1830-1836.
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PubMed id
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Secondary reference #3
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Title
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Crystal structure of basic 7s globulin, A xyloglucan-Specific endo-β-1,4-Glucanase inhibitor protein-Like protein from soybean lacking inhibitory activity against endo-β-Glucanase.
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Authors
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T.Yoshizawa,
T.Shimizu,
M.Yamabe,
M.Taichi,
Y.Nishiuchi,
N.Shichijo,
S.Unzai,
H.Hirano,
M.Sato,
H.Hashimoto.
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Ref.
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Febs J, 2011,
278,
1944-1954.
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PubMed id
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Secondary reference #4
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Title
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Internalisation and multiple phosphorylation of γ-Conglutin, The lupin seed glycaemia-Lowering protein, In hepg2 cells.
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Authors
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J.Capraro,
C.Magni,
F.Faoro,
D.Maffi,
A.Scarafoni,
G.Tedeschi,
E.Maffioli,
A.Parolari,
C.Manzoni,
M.R.Lovati,
M.Duranti.
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Ref.
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Biochem Biophys Res Commun, 2013,
437,
648-652.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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Lupin seed γ-Conglutin lowers blood glucose in hyperglycaemic rats and increases glucose consumption of hepg2 cells.
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Authors
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M.R.Lovati,
C.Manzoni,
S.Castiglioni,
A.Parolari,
C.Magni,
M.Duranti.
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Ref.
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Br J Nutr, 2012,
107,
67-73.
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PubMed id
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