X-ray structure of the SH3 domain of the phosphoinositide 3-kinase p85β subunit

Shuai Chen, Yibei Xiao, Rajesh Ponnusamy, Jinzhi Tan, Jian Lei, Rolf Hilgenfeld*

*Corresponding author for this work


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.

Original languageEnglish
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number11
Pages (from-to)1328-1333
Number of pages6
Publication statusPublished - 01.11.2011


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