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PDBsum entry 3a8p
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Signaling protein
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PDB id
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3a8p
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Contents |
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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Crystal structure of the tiam2 phccex domain
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Structure:
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T-lymphoma invasion and metastasis-inducing protein 2. Chain: a, b, c, d. Fragment: phccex domain, residues 500-757. Synonym: tiam-2, sif and tiam1-like exchange factor. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: tiam2, kiaa2016, stef. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.10Å
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R-factor:
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0.211
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R-free:
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0.253
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Authors:
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S.Terawaki,K.Kitano,T.Mori,Y.Zhai,Y.Higuchi,N.Itoh,T.Watanabe, K.Kaibuchi,T.Hakoshima
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Key ref:
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S.Terawaki
et al.
(2010).
The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.
Embo J,
29,
236-250.
PubMed id:
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Date:
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07-Oct-09
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Release date:
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24-Nov-09
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PROCHECK
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Headers
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References
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Q6ZPF3
(TIAM2_MOUSE) -
Rho guanine nucleotide exchange factor TIAM2 from Mus musculus
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Seq:
Struc:
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1715 a.a.
232 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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Embo J
29:236-250
(2010)
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PubMed id:
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The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.
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S.Terawaki,
K.Kitano,
T.Mori,
Y.Zhai,
Y.Higuchi,
N.Itoh,
T.Watanabe,
K.Kaibuchi,
T.Hakoshima.
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ABSTRACT
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Tiam1 and Tiam2 (Tiam1/2) are guanine nucleotide-exchange factors that possess
the PH-CC-Ex (pleckstrin homology, coiled coil and extra) region that mediates
binding to plasma membranes and signalling proteins in the activation of Rac
GTPases. Crystal structures of the PH-CC-Ex regions revealed a single globular
domain, PHCCEx domain, comprising a conventional PH subdomain associated with an
antiparallel coiled coil of CC subdomain and a novel three-helical globular Ex
subdomain. The PH subdomain resembles the beta-spectrin PH domain, suggesting
non-canonical phosphatidylinositol binding. Mutational and binding studies
indicated that CC and Ex subdomains form a positively charged surface for
protein binding. We identified two unique acidic sequence motifs in
Tiam1/2-interacting proteins for binding to PHCCEx domain, Motif-I in CD44 and
ephrinB's and the NMDA receptor, and Motif-II in Par3 and JIP2. Our results
suggest the molecular basis by which the Tiam1/2 PHCCEx domain facilitates dual
binding to membranes and signalling proteins.
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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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M.K.Hertweck,
F.Erdfelder,
and
K.A.Kreuzer
(2011).
CD44 in hematological neoplasias.
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Ann Hematol,
90,
493-508.
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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.
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Links
