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PDBsum entry 1yyh
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Cell cycle,transcription
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PDB id
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1yyh
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Cell cycle,transcription
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Title:
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Crystal structure of the human notch 1 ankyrin domain
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Structure:
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Notch 1, ankyrin domain. Chain: a, b. Fragment: ankyrin domain. Synonym: neurogenic locus notch homolog protein 1. Hn1. Translocation-associated notch protein tan-1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: notch1, tan1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.90Å
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R-factor:
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0.163
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R-free:
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0.193
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Authors:
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M.T.Ehebauer,D.Y.Chirgadze,P.Hayward,A.Martinez-Arias,T.L.Blundell
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Key ref:
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M.T.Ehebauer
et al.
(2005).
High-resolution crystal structure of the human Notch 1 ankyrin domain.
Biochem J,
392,
13-20.
PubMed id:
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Date:
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25-Feb-05
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Release date:
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16-Aug-05
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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.
193 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Biochem J
392:13-20
(2005)
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PubMed id:
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High-resolution crystal structure of the human Notch 1 ankyrin domain.
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M.T.Ehebauer,
D.Y.Chirgadze,
P.Hayward,
A.Martinez Arias,
T.L.Blundell.
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ABSTRACT
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The Notch receptor is part of a highly conserved signalling system of central
importance to animal development. Its ANK (ankyrin) domain is required for
Notch-mediated signal transduction. The crystal structure of the human Notch 1
ANK domain was solved by molecular replacement at 1.9 A (1 A=0.1 nm) resolution,
and it shows that the features identified in the Drosophila homologue are
conserved. The domain has six of the seven ANK repeats predicted from sequence.
The putative first repeat, which has only part of the consensus and a long
insertion, is disordered in both molecules in the asymmetric unit, possibly due
to the absence of the RAM (RBPJkappa-associated molecule) region N-terminal to
it. The exposed hydrophobic core is involved in intermolecular interactions in
the crystal. Evolutionary trace analysis identified several residues that map to
the hairpins of the structure and may be of functional importance. Based on the
Notch 1 ANK structure and analysis of homologous Notch ANK sequences, we predict
two possible binding sites on the domain: one on the concave surface of repeat 2
and the other below the hairpins of repeats 6-7.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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P.G.Sanders,
S.Muñoz-Descalzo,
T.Balayo,
F.Wirtz-Peitz,
P.Hayward,
and
A.M.Arias
(2009).
Ligand-independent traffic of Notch buffers activated Armadillo in Drosophila.
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PLoS Biol,
7,
e1000169.
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D.Fox,
I.Le Trong,
P.Rajagopal,
P.S.Brzovic,
R.E.Stenkamp,
and
R.E.Klevit
(2008).
Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences.
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J Biol Chem,
283,
21179-21186.
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PDB code:
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W.R.Gordon,
K.L.Arnett,
and
S.C.Blacklow
(2008).
The molecular logic of Notch signaling--a structural and biochemical perspective.
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J Cell Sci,
121,
3109-3119.
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D.F.Kelly,
R.J.Lake,
T.Walz,
and
S.Artavanis-Tsakonas
(2007).
Conformational variability of the intracellular domain of Drosophila Notch and its interaction with Suppressor of Hairless.
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Proc Natl Acad Sci U S A,
104,
9591-9596.
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M.A.Borzok,
D.H.Catino,
J.D.Nicholson,
A.Kontrogianni-Konstantopoulos,
and
R.J.Bloch
(2007).
Mapping the binding site on small ankyrin 1 for obscurin.
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J Biol Chem,
282,
32384-32396.
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M.L.Coleman,
M.A.McDonough,
K.S.Hewitson,
C.Coles,
J.Mecinovic,
M.Edelmann,
K.M.Cook,
M.E.Cockman,
D.E.Lancaster,
B.M.Kessler,
N.J.Oldham,
P.J.Ratcliffe,
and
C.J.Schofield
(2007).
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
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J Biol Chem,
282,
24027-24038.
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PDB codes:
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Y.Nam,
P.Sliz,
W.S.Pear,
J.C.Aster,
and
S.C.Blacklow
(2007).
Cooperative assembly of higher-order Notch complexes functions as a switch to induce transcription.
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Proc Natl Acad Sci U S A,
104,
2103-2108.
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K.Peng,
P.Radivojac,
S.Vucetic,
A.K.Dunker,
and
Z.Obradovic
(2006).
Length-dependent prediction of protein intrinsic disorder.
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BMC Bioinformatics,
7,
208.
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M.Kaspar,
and
T.Klein
(2006).
Functional analysis of murine CBF1 during Drosophila development.
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Dev Dyn,
235,
918-927.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
