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PDBsum entry 5fm9
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Transcription
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PDB id
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5fm9
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PDB id:
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Transcription
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Title:
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Human notch 1, egf 4-7
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Structure:
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Neurogenic locus notch homolog protein 1. Chain: a. Fragment: egf domains 4-7, unp residues 140-294. Synonym: notch 1, hn1, translocation-associated notch protein tan-1, notch 1 extracellular truncation, next, notch 1 intracellular domain, nicd. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.92Å
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R-factor:
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0.214
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R-free:
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0.237
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Authors:
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P.C.Weisshuhn,D.Sheppard,P.Taylor,P.Whiteman,S.M.Lea,P.A.Handford, C.Redfield
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Key ref:
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P.C.Weisshuhn
et al.
(2016).
Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies.
Structure,
24,
555-566.
PubMed id:
DOI:
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Date:
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02-Nov-15
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Release date:
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20-Apr-16
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PROCHECK
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Headers
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References
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P46531
(NOTC1_HUMAN) -
Neurogenic locus notch homolog protein 1 from Homo sapiens
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Seq: Struc:
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2555 a.a.
154 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Structure
24:555-566
(2016)
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PubMed id:
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Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies.
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P.C.Weisshuhn,
D.Sheppard,
P.Taylor,
P.Whiteman,
S.M.Lea,
P.A.Handford,
C.Redfield.
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ABSTRACT
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The Notch receptor is a key component of a core metazoan signaling pathway
activated by Delta/Serrate/Lag-2 ligands expressed on an adjacent cell. This
results in a short-range signal with profound effects on cell-fate
determination, cell proliferation, and cell death. Key to understanding receptor
function is structural knowledge of the large extracellular portion of Notch
which contains multiple repeats of epidermal growth factor (EGF)-like domains.
Here we investigate the EGF4-13 region of human Notch1 (hN1) using a
multidisciplinary approach. Ca(2+)-binding measurements, X-ray crystallography,
{(1)H}-(15)N heteronuclear nuclear Overhauser effects, and residual dipolar
couplings support a non-linear organization for the EGF4-13 region with a rigid,
bent conformation for EGF4-7 and a single flexible linkage between EGF9 and
EGF10. These data allow us to construct an informed model for EGF10-13 which, in
conjunction with comparative binding studies, demonstrates that EGF10 has an
important role in determining Notch receptor sensitivity to Dll-4.
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}
}
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