PDBsum entry 3mtt

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protein links
Signaling protein, protein binding PDB id
Protein chain
163 a.a. *
Waters ×14
* Residue conservation analysis
PDB id:
Name: Signaling protein, protein binding
Title: Crystal structure of ish2 domain of human p85beta, northeast structural genomics consortium target hr5531c
Structure: Phosphatidylinositol 3-kinase regulatory subunit chain: a. Fragment: ish2 domain, residues 433-610. Synonym: ptdins-3-kinase regulatory subunit beta, pi3-kinas regulatory subunit beta, pi3k regulatory subunit beta, phosphatidylinositol 3-kinase 85 kda regulatory subunit bet 3-kinase regulatory subunit p85-beta, pi3-kinase subunit p8 engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pik3r2. Expressed in: escherichia coli. Expression_system_taxid: 511693.
3.30Å     R-factor:   0.250     R-free:   0.277
Authors: R.Guan,C.Schauder,L.C.Ma,R.M.Krug,G.T.Montelione,Northeast S Genomics Consortium (Nesg)
Key ref: C.Schauder et al. (2010). Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85β subunit reveals conformational plasticity in the interhelical turn region. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 1567-1571. PubMed id: 21139197
30-Apr-10     Release date:   19-May-10    
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Protein chain
Pfam   ArchSchema ?
O00459  (P85B_HUMAN) -  Phosphatidylinositol 3-kinase regulatory subunit beta
728 a.a.
163 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     phosphatidylinositol 3-kinase complex   1 term 
  Biochemical function     phosphatidylinositol 3-kinase regulator activity     1 term  


Acta Crystallogr Sect F Struct Biol Cryst Commun 66:1567-1571 (2010)
PubMed id: 21139197  
Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85β subunit reveals conformational plasticity in the interhelical turn region.
C.Schauder, L.C.Ma, R.M.Krug, G.T.Montelione, R.Guan.
Phosphatidylinositol 3-kinase (PI3K) proteins actively trigger signaling pathways leading to cell growth, proliferation and survival. These proteins have multiple isoforms and consist of a catalytic p110 subunit and a regulatory p85 subunit. The iSH2 domain of the p85β isoform has been implicated in the binding of nonstructural protein 1 (NS1) of influenza A viruses. Here, the crystal structure of human p85β iSH2 determined to 3.3 Å resolution is reported. The structure reveals that this domain mainly consists of a coiled-coil motif. Comparison with the published structure of the bovine p85β iSH2 domain bound to the influenza A virus nonstructural protein 1 indicates that little or no structural change occurs upon complex formation. By comparing this human p85β iSH2 structure with the bovine p85β iSH2 domain, which shares 99% sequence identity, and by comparing the multiple conformations observed within the asymmetric unit of the bovine iSH2 structure, it was found that this coiled-coil domain exhibits a certain degree of conformational variability or `plasticity' in the interhelical turn region. It is speculated that this plasticity of p85β iSH2 may play a role in regulating its functional and molecular-recognition properties.