1H and 15N assignments and secondary structure of the PI3K SH3 domain

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

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The sequential 1H and 15N assignments of the SH3 domain of human phosphatidyl inositol 3'-kinase (PI3K) were determined by a combination of homonuclear and heteronuclear NMR experiments. With the exception of several protons belonging to lysine and proline residues, all proton and proton-bearing amide nitrogen resonances were assigned. Based on the sequential nuclear Overhauser effects (NOEs), 3JNH-CαH coupling constants and locations of slowly exchanging amide protons, we determined that the secondary structures of the protein consists of six β-strands, two β-turns and four short helices. Additional long range NOEs indicate that these β-strands form two antiparallel β-sheets. The topology of secondary structural elements of the PI3K SH3 domain is similar to those of the SH3 domains from c-Src and α-spectrin, suggesting that the SH3 family has a common tertiary structural motif.

Original languageEnglish (US)
Pages (from-to)93-98
Number of pages6
JournalFEBS Letters
Volume324
Issue number1
DOIs
StatePublished - Jun 7 1993

Keywords

  • Nuclear magnetic resonance: Secondary structure
  • PI3K
  • SH3 domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Koyama, S., Yu, H., Dalgarno, D. C., Shin, T. B., Zydowsky, L. D., & Schreiber, S. L. (1993). 1H and 15N assignments and secondary structure of the PI3K SH3 domain. FEBS Letters, 324(1), 93-98. https://doi.org/10.1016/0014-5793(93)81539-C