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PDBsum entry 1vf6
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Protein binding/protein transport
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PDB id
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1vf6
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Contents |
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58 a.a.
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60 a.a.
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51 a.a.
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48 a.a.
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* Residue conservation analysis
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PDB id:
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Protein binding/protein transport
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Title:
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2.1 angstrom crystal structure of the pals-1-l27n and patj l27 heterodimer complex
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Structure:
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Pals1-associated tight junction protein. Chain: a, b. Fragment: l27n domain. Synonym: pals-1. Engineered: yes. Maguk p55 subfamily member 5. Chain: c, d. Fragment: l27 domain. Synonym: patj, protein associated with lin-7 1.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Mus musculus. House mouse. Organism_taxid: 10090.
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Biol. unit:
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24mer (from
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Resolution:
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2.10Å
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R-factor:
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0.242
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R-free:
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0.262
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Authors:
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Y.Li,A.Lavie,B.Margolis,D.Karnak
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Key ref:
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Y.Li
et al.
(2004).
Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes.
EMBO J,
23,
2723-2733.
PubMed id:
DOI:
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Date:
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09-Apr-04
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Release date:
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20-Apr-04
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PROCHECK
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Headers
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References
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Q8NI35
(INADL_HUMAN) -
InaD-like protein from Homo sapiens
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Seq:
Struc:
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1801 a.a.
58 a.a.*
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Q8NI35
(INADL_HUMAN) -
InaD-like protein from Homo sapiens
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Seq:
Struc:
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1801 a.a.
60 a.a.*
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DOI no:
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EMBO J
23:2723-2733
(2004)
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PubMed id:
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Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes.
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Y.Li,
D.Karnak,
B.Demeler,
B.Margolis,
A.Lavie.
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ABSTRACT
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L27 is a protein-binding domain that can assemble essential proteins for
signaling and cell polarity into complexes by interacting in a heterodimeric
manner. One of these protein complexes is the PATJ/PALS1/Crumbs tripartite
complex, which is crucial for the establishment and maintenance of cell
polarity. To reveal the structural basis underlining the obligate
heterodimerization, we have determined the crystal structure of the
PALS1-L27N/PATJ-L27 heterodimer complex. Each L27 domain is composed of three
helices. The two L27 domains heterodimerize by building a compact structure
consisting of a four-helix bundle formed by the first two helices of each L27
domain and one coiled-coil formed by the third helix of each domain. The large
hydrophobic packing interactions contributed by all the helices of both L27
domains predominantly drive the heterodimer formation, which is likely to be a
general feature of L27 domains. Combined with mutational studies, we can begin
to understand the structural basis for the specificity of L27 binding pairs. Our
results provide unique insights into L27 domain heterodimer complex, which is
critical for cell polarization.
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Selected figure(s)
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Figure 2.
Figure 2 Structure of the L27[PALS1N]/L27[PATJ] heterodimer. (A)
Overall structure of the two PALS1 -PATJ L27 domain complexes
present in the crystallographic asymmetric unit. Red/yellow:
PALS1; blue/green: PATJ. (B) Ribbon diagram of the SAP97 L27 and
the mLin2 L27N complex solved by NMR (Feng et al, 2004). Based
on sequence alignment (Figure 1B) and domain classification, the
SAP97 L27 domain is colored in blue and green, analogous to the
PATJ L27 domain, whereas mLin2 is colored in red and yellow,
analogous to the PALS1 L27N domain. Note the similarity in the
heterodimer formation to that of the L27[PALS1N]/L27[PATJ]
heterodimer, and the striking difference in the interface
between the two heterodimers. (C) Overlay of the two
heterodimers in the asymmetric unit based on C  atoms
belonging to Helix 1 and Helix 2 of the PATJ L27 domain.
Red/yellow: PALS1; blue/green: PATJ. (D) Overlay of the two
heterodimers in the asymmetric unit based on C atoms
from Helix 3 of the PATJ L27 domain. All structural figures were
generated with MOLSCRIPT (Kraulis, 1991) and RASTER3D (Merrit
and Murphy, 1994).
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Figure 3.
Figure 3 Comparison of the L27[PALS1N] and L27[PATJ] domains.
Ribbon diagram of the PATJ L27 domain (A) and of the PALS1 L27
domain (B). (C) Stereoview of a C trace
of the overlaid L27[PALS1N] and L27[PATJ] domains. Red/yellow:
PALS1; blue/green: PATJ. (The red and blue belong to one
heterodimer in the asymmetric unit, and yellow and green belong
to the other copy.) 
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
2723-2733)
copyright 2004.
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Figures were
selected
by an automated process.
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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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O.Olsen,
L.Funke,
J.F.Long,
M.Fukata,
T.Kazuta,
J.C.Trinidad,
K.A.Moore,
H.Misawa,
P.A.Welling,
A.L.Burlingame,
M.Zhang,
and
D.S.Bredt
(2007).
Renal defects associated with improper polarization of the CRB and DLG polarity complexes in MALS-3 knockout mice.
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J Cell Biol,
179,
151-164.
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C.Alewine,
O.Olsen,
J.B.Wade,
and
P.A.Welling
(2006).
TIP-1 has PDZ scaffold antagonist activity.
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Mol Biol Cell,
17,
4200-4211.
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C.Cai,
H.Li,
C.Rivera,
and
K.Keinänen
(2006).
Interaction between SAP97 and PSD-95, two Maguk proteins involved in synaptic trafficking of AMPA receptors.
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J Biol Chem,
281,
4267-4273.
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S.W.Straight,
J.N.Pieczynski,
E.L.Whiteman,
C.J.Liu,
and
B.Margolis
(2006).
Mammalian lin-7 stabilizes polarity protein complexes.
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J Biol Chem,
281,
37738-37747.
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K.Y.Petrosky,
H.D.Ou,
F.Löhr,
V.Dötsch,
and
W.A.Lim
(2005).
A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes.
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J Biol Chem,
280,
38528-38536.
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PDB code:
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W.Feng,
J.F.Long,
and
M.Zhang
(2005).
A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins.
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Proc Natl Acad Sci U S A,
102,
6861-6866.
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PDB codes:
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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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