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 language | English (US) |
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Pages (from-to) | 93-98 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 324 |
Issue number | 1 |
DOIs | |
State | Published - 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