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PDBsum entry 1y7n
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Protein transport
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PDB id
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1y7n
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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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Protein transport
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Title:
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Solution structure of the second pdz domain of the human neuronal adaptor x11alpha
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Structure:
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Amyloid beta a4 precursor protein-binding family a member 1. Chain: a. Fragment: second pdz domain. Synonym: neuron-specific x11 protein, neuronal munc18-1-interacting protein 1, mint-1, adapter protein x11alpha. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Tissue: brain. Gene: apba1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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A.E.Duquesne,M.De Ruijter,J.Brouwer,J.W.Drijfhout,S.B.Nabuurs, C.A.E.M.Spronk,G.W.Vuister,M.Ubbink,G.W.Canters
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Key ref:
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A.E.Duquesne
et al.
(2005).
Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C-terminal peptide of the human copper chaperone for superoxide dismutase.
J Biomol Nmr,
32,
209-218.
PubMed id:
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Date:
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09-Dec-04
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Release date:
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22-Nov-05
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PROCHECK
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Headers
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References
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Q02410
(APBA1_HUMAN) -
Amyloid-beta A4 precursor protein-binding family A member 1 from Homo sapiens
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Seq:
Struc:
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837 a.a.
84 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 5 residue positions (black
crosses)
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J Biomol Nmr
32:209-218
(2005)
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PubMed id:
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Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C-terminal peptide of the human copper chaperone for superoxide dismutase.
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A.E.Duquesne,
M.d.Ruijter,
J.Brouwer,
J.W.Drijfhout,
S.B.Nabuurs,
C.A.Spronk,
G.W.Vuister,
M.Ubbink,
G.W.Canters.
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ABSTRACT
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Protection against reactive oxygen species is provided by the copper containing
enzyme superoxide dismutase 1 (SOD1). The copper chaperone CCS is responsible
for copper insertion into apo-SOD1. This role is impaired by an interaction
between the second PDZ domain (PDZ2alpha) of the neuronal adaptor protein
X11alpha and the third domain of CCS (McLoughlin et al. (2001) J. Biol. Chem.,
276, 9303-9307). The solution structure of the PDZ2alpha domain has been
determined and the interaction with peptides derived from CCS has been explored.
PDZ2alpha binds to the last four amino acids of the CCS protein (PAHL) with a
dissociation constant of 91 +/- 2 microM. Peptide variants have been used to map
the interaction areas on PDZ2alpha for each amino acid, showing an important
role for the C-terminal leucine, in line with canonical PDZ-peptide interactions.
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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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A.Swistowski,
Q.Zhang,
M.E.Orcholski,
D.Crippen,
C.Vitelli,
A.Kurakin,
and
D.E.Bredesen
(2009).
Novel mediators of amyloid precursor protein signaling.
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J Neurosci,
29,
15703-15712.
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R.Schmucki,
S.Yokoyama,
and
P.Güntert
(2009).
Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm.
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J Biomol NMR,
43,
97.
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E.Saccenti,
and
A.Rosato
(2008).
The war of tools: how can NMR spectroscopists detect errors in their structures?
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J Biomol NMR,
40,
251-261.
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B.Rogelj,
J.C.Mitchell,
C.C.Miller,
and
D.M.McLoughlin
(2006).
The X11/Mint family of adaptor proteins.
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Brain Res Rev,
52,
305-315.
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C.C.Miller,
D.M.McLoughlin,
K.F.Lau,
M.E.Tennant,
and
B.Rogelj
(2006).
The X11 proteins, Abeta production and Alzheimer's disease.
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Trends Neurosci,
29,
280-285.
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H.Kusunoki,
and
T.Kohno
(2006).
Solution structure of human erythroid p55 PDZ domain.
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Proteins,
64,
804-807.
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PDB code:
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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
