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PDBsum entry 3o5z

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protein ligands metals Protein-protein interface(s) links
Protein binding PDB id
3o5z
Jmol
Contents
Protein chains
82 a.a.
78 a.a.
Ligands
MPD
Metals
_CL ×2
Waters ×23
PDB id:
3o5z
Name: Protein binding
Title: Crystal structure of the sh3 domain from p85beta subunit of phosphoinositide 3-kinase (pi3k)
Structure: Phosphatidylinositol 3-kinase regulatory subunit chain: a, b. Fragment: sh3 domain, unp residues 6-90. 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: 562
Resolution:
2.01Å     R-factor:   0.216     R-free:   0.259
Authors: S.Chen,Y.Xiao,R.Ponnusamy,J.Tan,J.Lei,R.Hilgenfeld
Key ref: S.Chen et al. (2011). X-ray structure of the SH3 domain of the phosphoinositide 3-kinase p85β subunit. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 1328-1333. PubMed id: 22102226 DOI: 10.1107/S1744309111031691
Date:
28-Jul-10     Release date:   10-Aug-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O00459  (P85B_HUMAN) -  Phosphatidylinositol 3-kinase regulatory subunit beta
Seq:
Struc:
 
Seq:
Struc:
728 a.a.
82 a.a.
Protein chain
Pfam   ArchSchema ?
O00459  (P85B_HUMAN) -  Phosphatidylinositol 3-kinase regulatory subunit beta
Seq:
Struc:
 
Seq:
Struc:
728 a.a.
78 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

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

 

 
DOI no: 10.1107/S1744309111031691 Acta Crystallogr Sect F Struct Biol Cryst Commun 67:1328-1333 (2011)
PubMed id: 22102226  
 
 
X-ray structure of the SH3 domain of the phosphoinositide 3-kinase p85β subunit.
S.Chen, Y.Xiao, R.Ponnusamy, J.Tan, J.Lei, R.Hilgenfeld.
 
  ABSTRACT  
 
Src-homology 3 (SH3) domains are involved in extensive protein-protein interactions and constitute key elements of intracellular signal transduction. Three-dimensional structures have been reported for SH3 domains of various proteins, including the 85 kDa regulatory subunit (p85) of phosphoinositide 3-kinase. However, all of the latter structures are of p85 isoform α and no crystal structure of the SH3 domain of the equally important isoform β has been reported to date. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.0 Å resolution of the SH3 domain of human p85β is described. The structure reveals a compact β-barrel fold very similar to that of p85α. However, binding studies with two classes of proline-rich ligand peptides demonstrate that the ligand-binding specificity differs slightly between the SH3 domains of human p85β and p85α, despite their high structural similarity.