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PDBsum entry 4ey0

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protein Protein-protein interface(s) links
Hydrolase PDB id
4ey0
Jmol
Contents
Protein chains
235 a.a.
Waters ×163
PDB id:
4ey0
Name: Hydrolase
Title: Structure of tandem sh2 domains from plcgamma1
Structure: 1-phosphatidylinositol 4,5-bisphosphate phosphodi gamma-1. Chain: a, b, c, d. Synonym: plc-148, phosphoinositide phospholipasE C-gamma-1, phospholipasE C-ii, plc-ii, phospholipasE C-gamma-1, plc-ga engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: plc1, plcg1. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.80Å     R-factor:   0.199     R-free:   0.242
Authors: A.R.Cole,C.P.Mas-Droux,T.D.Bunney,M.Katan
Key ref: T.D.Bunney et al. (2012). Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structure, 20, 2062-2075. PubMed id: 23063561
Date:
01-May-12     Release date:   31-Oct-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P19174  (PLCG1_HUMAN) -  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1290 a.a.
235 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.1.4.11  - Phosphoinositide phospholipase C.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
myo-Inositol Phosphate Metabolism
      Reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
+ H(2)O
= 1D-myo-inositol 1,4,5-trisphosphate
+ diacylglycerol
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     intracellular signal transduction   2 terms 
  Biochemical function     phosphatidylinositol phospholipase C activity     1 term  

 

 
    reference    
 
 
Structure 20:2062-2075 (2012)
PubMed id: 23063561  
 
 
Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation.
T.D.Bunney, D.Esposito, C.Mas-Droux, E.Lamber, R.W.Baxendale, M.Martins, A.Cole, D.Svergun, P.C.Driscoll, M.Katan.
 
  ABSTRACT  
 
Multidomain proteins incorporating interaction domains are central to regulation of cellular processes. The elucidation of structural organization and mechanistic insights into many of these proteins, however, remain challenging due to their inherent flexibility. Here, we describe the organization and function of four interaction domains in PLCγ1 using a combination of structural biology and biochemical approaches. Intramolecular interactions within the regulatory region center on the cSH2 domain, the only domain that also interacts with the PLC-core. In the context of fibroblast growth-factor receptor signaling, the coordinated involvement of nSH2 and cSH2 domains mediates efficient phosphorylation of PLCγ1 resulting in the interruption of an autoinhibitory interface by direct competition and, independently, dissociation of PLCγ1 from the receptor. Further structural insights into the autoinhibitory surfaces provide a framework to interpret gain-of-function mutations in PLCγ isoforms linked to immune disorders and illustrate a distinct mechanism for regulation of PLC activity by common interaction domains.