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PDBsum entry 3a8n

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Signaling protein PDB id
3a8n

 

 

 

 

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Contents
Protein chain
230 a.a. *
* Residue conservation analysis
PDB id:
3a8n
Name: Signaling protein
Title: Crystal structure of the tiam1 phccex domain
Structure: T-lymphoma invasion and metastasis-inducing protein 1. Chain: a. Fragment: phccex domain, residues 429-702. Synonym: tiam-1. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: tiam1, tiam-1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
4.50Å     R-factor:   0.306     R-free:   0.396
Authors: S.Terawaki,K.Kitano,T.Mori,Y.Zhai,Y.Higuchi,N.Itoh,T.Watanabe, K.Kaibuchi,T.Hakoshima
Key ref: 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: 19893486
Date:
07-Oct-09     Release date:   24-Nov-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q60610  (TIAM1_MOUSE) -  Rho guanine nucleotide exchange factor TIAM1 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1591 a.a.
230 a.a.
Key:    PfamA domain  Secondary structure

 

 
Embo J 29:236-250 (2010)
PubMed id: 19893486  
 
 
The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.
S.Terawaki, K.Kitano, T.Mori, Y.Zhai, Y.Higuchi, N.Itoh, T.Watanabe, K.Kaibuchi, T.Hakoshima.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21258793 M.K.Hertweck, F.Erdfelder, and K.A.Kreuzer (2011).
CD44 in hematological neoplasias.
  Ann Hematol, 90, 493-508.  
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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