PDBsum entry 4ey0

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protein Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
235 a.a.
Waters ×163
PDB id:
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
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 DOI: 10.1016/j.str.2012.09.005
01-May-12     Release date:   31-Oct-12    
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Protein chains
Pfam   ArchSchema ?
P19174  (PLCG1_HUMAN) -  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
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)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     intracellular signal transduction   2 terms 
  Biochemical function     phosphatidylinositol phospholipase C activity     1 term  


DOI no: 10.1016/j.str.2012.09.005 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.
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.