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PDBsum entry 3e17
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Cell adhesion
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PDB id
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3e17
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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 adhesion
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Title:
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Crystal structure of the second pdz domain from human zona occludens-2
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Structure:
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Tight junction protein zo-2. Chain: a, b. Fragment: unp residues 306-384. Synonym: zonula occludens protein 2, zona occludens protein 2, tight junction protein 2, the second pdz domain from human zona occludens- 2. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: tjp2, x104, zo2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.75Å
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R-factor:
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0.208
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R-free:
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0.237
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Authors:
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H.Chen,S.L.Tong,M.K.Teng,L.W.Niu
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Key ref:
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H.Chen
et al.
(2009).
Structure of the second PDZ domain from human zonula occludens 2.
Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
327-330.
PubMed id:
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Date:
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01-Aug-08
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Release date:
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21-Jul-09
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PROCHECK
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Headers
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References
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Q9UDY2
(ZO2_HUMAN) -
Tight junction protein ZO-2 from Homo sapiens
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Seq: Struc:
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1190 a.a.
80 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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Acta Crystallogr Sect F Struct Biol Cryst Commun
65:327-330
(2009)
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PubMed id:
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Structure of the second PDZ domain from human zonula occludens 2.
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H.Chen,
S.Tong,
X.Li,
J.Wu,
Z.Zhu,
L.Niu,
M.Teng.
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ABSTRACT
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Human zonula occludens 2 (ZO-2) protein is a multi-domain protein that consists
of an SH3 domain, a GK domain and three copies of a PDZ domain with slight
divergence. The three PDZ domains act as protein-recognition modules that may
mediate protein assembly and subunit localization. The crystal structure of the
second PDZ domain of ZO-2 (ZO-2 PDZ2) was determined by molecular replacement at
1.75 A resolution, revealing a dimer in the asymmetric unit. The dimer is
stabilized by extensive symmetrical domain-swapping of the beta1 and beta2
strands. Structural comparison shows that the ZO-2 PDZ2 homodimer may have a
similar ligand-binding pattern to the ZO-1 PDZ2-connexin 43 complex.
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');
}
}
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