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PDBsum entry 2emt
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Cell adhesion
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PDB id
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2emt
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Contents |
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* Residue conservation analysis
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PDB id:
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Cell adhesion
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Title:
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Crystal structure analysis of the radixin ferm domain complexed with adhesion molecule psgl-1
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Structure:
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Radixin. Chain: a, b. Fragment: n-terminal ferm domain (residues 1-310). Synonym: esp10. Engineered: yes. P-selectin glycoprotein ligand 1. Chain: c, d, e. Fragment: psgl-1 cytoplasmic peptide, 18 n-terminal residues of the cytoplasmic tail.
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence occurs naturally in mouse.
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Resolution:
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2.80Å
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R-factor:
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0.235
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R-free:
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0.294
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Authors:
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Y.Takai,K.Kitano,S.Terawaki,R.Maesaki,T.Hakoshima
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Key ref:
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Y.Takai
et al.
(2007).
Structural basis of PSGL-1 binding to ERM proteins.
Genes Cells,
12,
1329-1338.
PubMed id:
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Date:
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28-Mar-07
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Release date:
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18-Mar-08
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PROCHECK
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Headers
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References
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P26043
(RADI_MOUSE) -
Radixin from Mus musculus
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Seq:
Struc:
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583 a.a.
313 a.a.*
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Genes Cells
12:1329-1338
(2007)
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PubMed id:
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Structural basis of PSGL-1 binding to ERM proteins.
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Y.Takai,
K.Kitano,
S.Terawaki,
R.Maesaki,
T.Hakoshima.
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ABSTRACT
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P-selectin glycoprotein ligand-1 (PSGL-1), an adhesion molecule with
O-glycosylated extracellular sialomucins, is involved in leukocyte inflammatory
responses. On activation, ezrin-radixin-moesin (ERM) proteins mediate the
redistribution of PSGL-1 on polarized cell surfaces to facilitate binding to
target molecules. ERM proteins recognize a short binding motif, Motif-1,
conserved in cytoplasmic tails of adhesion molecules, whereas PSGL-1 lacks
Motif-1 residues important for binding to ERM proteins. The crystal structure of
the complex between the radixin FERM domain and a PSGL-1 juxtamembrane peptide
reveals that the peptide binds the groove of FERM subdomain C by forming a
beta-strand associated with strand beta5C, followed by a loop flipped out
towards the solvent. The Motif-1 3(10) helix present in the FERM-ICAM-2 complex
is absent in PSGL-1 given the absence of a critical Motif-1 alanine residue, and
PSGL-1 reduces its contact area with subdomain C. Non-conserved positions are
occupied by large residues Met9 and His8, which stabilize peptide conformation
and enhance groove binding. Non-conserved residues play an important role in
compensating for loss of binding energy resulting from the absence of conserved
residues important for binding.
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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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Z.Wei,
J.Yan,
Q.Lu,
L.Pan,
and
M.Zhang
(2011).
Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain.
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Proc Natl Acad Sci U S A,
108,
3572-3577.
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PDB code:
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R.G.Fehon,
A.I.McClatchey,
and
A.Bretscher
(2010).
Organizing the cell cortex: the role of ERM proteins.
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Nat Rev Mol Cell Biol,
11,
276-287.
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S.Terawaki,
K.Kitano,
T.Mori,
Y.Zhai,
Y.Higuchi,
N.Itoh,
T.Watanabe,
K.Kaibuchi,
and
T.Hakoshima
(2010).
The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.
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EMBO J,
29,
236-250.
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PDB codes:
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D.J.Killock,
M.Parsons,
M.Zarrouk,
S.M.Ameer-Beg,
A.J.Ridley,
D.O.Haskard,
M.Zvelebil,
and
A.Ivetic
(2009).
In Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin.
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J Biol Chem,
284,
8833-8845.
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M.Y.Niv,
K.Iida,
R.Zheng,
A.Horiguchi,
R.Shen,
and
D.M.Nanus
(2009).
Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.
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Protein Sci,
18,
1042-1050.
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J.J.Miner,
L.Xia,
T.Yago,
J.Kappelmayer,
Z.Liu,
A.G.Klopocki,
B.Shao,
J.M.McDaniel,
H.Setiadi,
D.W.Schmidtke,
and
R.P.McEver
(2008).
Separable requirements for cytoplasmic domain of PSGL-1 in leukocyte rolling and signaling under flow.
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Blood,
112,
2035-2045.
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S.Terawaki,
K.Kitano,
M.Aoyama,
and
T.Hakoshima
(2008).
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP).
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
911-913.
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T.Mori,
K.Kitano,
S.Terawaki,
R.Maesaki,
Y.Fukami,
and
T.Hakoshima
(2008).
Structural basis for CD44 recognition by ERM proteins.
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J Biol Chem,
283,
29602-29612.
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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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