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Title
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1H and 15N assignments and secondary structure of the PI3K SH3 domain.
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Authors
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S.Koyama,
H.Yu,
D.C.Dalgarno,
T.B.Shin,
L.D.Zydowsky,
S.L.Schreiber.
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Ref.
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Febs Lett, 1993,
324,
93-98.
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PubMed id
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Abstract
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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-C alpha H coupling constants and locations of slowly exchanging
amide protons, we determined that the secondary structures of the protein
consists of six beta-strands, two beta-turns and four short helices. Additional
long range NOEs indicate that these beta-strands form two antiparallel
beta-sheets. The topology of secondary structural elements of the PI3K SH3
domain is similar to those of the SH3 domains from c-Src and alpha-spectrin,
suggesting that the SH3 family has a common tertiary structural motif.
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