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PDBsum entry 4xlw
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Protein binding
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PDB id
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4xlw
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References listed in PDB file
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Key reference
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Title
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Structural biology. Structural basis for notch1 engagement of delta-Like 4.
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Authors
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V.C.Luca,
K.M.Jude,
N.W.Pierce,
M.V.Nachury,
S.Fischer,
K.C.Garcia.
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Ref.
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Science, 2015,
347,
847-853.
[DOI no: ]
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PubMed id
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Abstract
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Notch receptors guide mammalian cell fate decisions by engaging the proteins
Jagged and Delta-like (DLL). The 2.3 angstrom resolution crystal structure of
the interacting regions of the Notch1-DLL4 complex reveals a two-site,
antiparallel binding orientation assisted by Notch1 O-linked glycosylation.
Notch1 epidermal growth factor-like repeats 11 and 12 interact with the DLL4
Delta/Serrate/Lag-2 (DSL) domain and module at the N-terminus of Notch ligands
(MNNL) domains, respectively. Threonine and serine residues on Notch1 are
functionalized with O-fucose and O-glucose, which act as surrogate amino acids
by making specific, and essential, contacts to residues on DLL4. The elucidation
of a direct chemical role for O-glycans in Notch1 ligand engagement demonstrates
how, by relying on posttranslational modifications of their ligand binding
sites, Notch proteins have linked their functional capacity to developmentally
regulated biosynthetic pathways.
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