Structure of the Pl3K SH3 domain and analysis of the SH3 family

Satoshi Koyama, Hongtao Yu, David C. Dalgarno, Tae Bum Shin, Lynne D. Zydowsky, Stuart L. Schreiber

Research output: Contribution to journalArticle

121 Scopus citations

Abstract

Src homology 3 (SH3) domains, which are found in many proteins involved in intracellular signal transduction, mediate specific protein-protein interactions. The three-dimensional structure of the SH3 domain in the p85 subunit of the phosphatidylinositol 3-kinase (Pl3K) has been determined by multidimensional NMR methods. The molecule consists of four short helices, two β turns, and two antiparallel β sheets. The β sheets are highly similar to corresponding regions in the SH3 domain of the tyrosine kinase Src, even though the sequence identity of the two domains is low. There is a unique 15 amino acid insert in Pl3K that contains three short helices. There are substantial differences in the identity of the amino acids that make up the receptor site of SH3 domains. The results suggest that while the overall structures of the binding sites in the Pl3K and Src SH3 domains are similar, their ligand binding properties may differ.

Original languageEnglish (US)
Pages (from-to)945-952
Number of pages8
JournalCell
Volume72
Issue number6
DOIs
StatePublished - Mar 26 1993

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Koyama, S., Yu, H., Dalgarno, D. C., Shin, T. B., Zydowsky, L. D., & Schreiber, S. L. (1993). Structure of the Pl3K SH3 domain and analysis of the SH3 family. Cell, 72(6), 945-952. https://doi.org/10.1016/0092-8674(93)90582-B