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PDBsum entry 2awx
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Membrane protein
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PDB id
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2awx
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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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Membrane protein
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Title:
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Synapse associated protein 97 pdz2 domain variant c378s
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Structure:
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Synapse associated protein 97. Chain: a, b. Fragment: pdz2 domain. Synonym: presynaptic protein sap97, sap-97. Engineered: yes. Mutation: yes
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: dlg1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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1.80Å
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R-factor:
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0.191
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R-free:
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0.254
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Authors:
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I.Von Ossowski,E.Oksanen,L.Von Ossowski,C.Cai,M.Sundberg,A.Goldman, K.Keinanen
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Key ref:
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I.von Ossowski
et al.
(2006).
Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide.
Febs J,
273,
5219-5229.
PubMed id:
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Date:
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02-Sep-05
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Release date:
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29-Aug-06
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PROCHECK
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Headers
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References
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Q62696
(DLG1_RAT) -
Disks large homolog 1 from Rattus norvegicus
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Seq:
Struc:
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911 a.a.
92 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 4 residue positions (black
crosses)
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Febs J
273:5219-5229
(2006)
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PubMed id:
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Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide.
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I.von Ossowski,
E.Oksanen,
L.von Ossowski,
C.Cai,
M.Sundberg,
A.Goldman,
K.Keinänen.
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ABSTRACT
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Synaptic targeting of GluR-A subunit-containing glutamate receptors involves an
interaction with synapse-associated protein 97 (SAP97). The C-terminus of
GluR-A, which contains a class I PDZ ligand motif (-x-Ser/Thr-x-phi-COOH where
phi is an aliphatic amino acid) associates preferentially with the second PDZ
domain of SAP97 (SAP97(PDZ2)). To understand the structural basis of this
interaction, we have determined the crystal structures of wild-type and a
SAP97(PDZ2) variant in complex with an 18-mer C-terminal peptide (residues
890-907) of GluR-A and of two variant PDZ2 domains in unliganded state at
1.8-2.44 A resolutions. SAP97(PDZ2) folds to a compact globular domain
comprising six beta-strands and two alpha-helices, a typical architecture for
PDZ domains. In the structure of the peptide complex, only the last four
C-terminal residues of the GluR-A are visible, and align as an antiparallel
beta-strand in the binding groove of SAP97(PDZ2). The free carboxylate group and
the aliphatic side chain of the C-terminal leucine (Leu907), and the hydroxyl
group of Thr905 of the GluR-A peptide are engaged in essential class I PDZ
interactions. Comparison between the free and complexed structures reveals
conformational changes which take place upon peptide binding. The
betaAlpha-betaBeta loop moves away from the C-terminal end of alphaB leading to
a slight opening of the binding groove, which may better accommodate the peptide
ligand. The two conformational states are stabilized by alternative hydrogen
bond and coulombic interactions of Lys324 in betaAlpha-betaBeta loop with Asp396
or Thr394 in betaBeta. Results of in vitro binding and immunoprecipitation
experiments using a PDZ motif-destroying L907A mutation as well as the insertion
of an extra alanine residue between the C-terminal Leu907 and the stop codon are
also consistent with a 'classical' type I PDZ interaction between SAP97 and
GluR-A C-terminus.
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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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B.Balana,
I.Maslennikov,
W.Kwiatkowski,
K.M.Stern,
L.Bahima,
S.Choe,
and
P.A.Slesinger
(2011).
Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27.
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Proc Natl Acad Sci U S A,
108,
5831-5836.
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PDB codes:
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K.Kaufmann,
N.Shen,
L.Mizoue,
and
J.Meiler
(2011).
A physical model for PDZ-domain/peptide interactions.
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J Mol Model,
17,
315-324.
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O.Sakarya,
C.Conaco,
O.Egecioglu,
S.A.Solla,
T.H.Oakley,
and
K.S.Kosik
(2010).
Evolutionary expansion and specialization of the PDZ domains.
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Mol Biol Evol,
27,
1058-1069.
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H.S.Carr,
C.Cai,
K.Keinänen,
and
J.A.Frost
(2009).
Interaction of the RhoA exchange factor Net1 with discs large homolog 1 protects it from proteasome-mediated degradation and potentiates Net1 activity.
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J Biol Chem,
284,
24269-24280.
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J.Liu,
J.Zhang,
Y.Yang,
H.Huang,
W.Shen,
Q.Hu,
X.Wang,
J.Wu,
and
Y.Shi
(2008).
Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor.
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Protein Sci,
17,
1003-1014.
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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
codes are
shown on the right.
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Links
