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PDBsum entry 1pkt
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Phosphotransferase
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PDB id
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1pkt
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References listed in PDB file
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Key reference
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Title
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Structure of the pi3k sh3 domain and analysis of the sh3 family.
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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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Cell, 1993,
72,
945-952.
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PubMed id
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Abstract
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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 (PI3K) has been determined by
multidimensional NMR methods. The molecule consists of four short helices, two
beta turns, and two antiparallel beta sheets. The beta 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 PI3K 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 PI3K and Src SH3 domains are similar,
their ligand binding properties may differ.
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Secondary reference #1
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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.
[DOI no: ]
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PubMed id
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Figure 3.
Fig. 3. A schematic diagram of the inter-strand NOES m the p-sheet regions of the I3K SH3 domain. Solid lines indicate inter-strand NOES and
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Figure 5.
FEBS Lett. 307. 55-61.
[3] Willams, L.T. (1992) Crr. iol. 2, 6Oll60.
[4] Lowenstein. E.J.. Daly, R.J., Datzer, A.G.. Li. W., Margohs. B.,
Lammers, R , Ullrich. A.L., Skolnik. F.Y.. Bar-Sag, H. and Sch-
lessmger, J. (1992) Cel 70, 431442.
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The above figures are
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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