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PDBsum entry 1shf
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Phosphotransferase
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PDB id
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1shf
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the sh3 domain in human fyn; comparison of the three-Dimensional structures of sh3 domains in tyrosine kinases and spectrin.
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Authors
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M.E.Noble,
A.Musacchio,
M.Saraste,
S.A.Courtneidge,
R.K.Wierenga.
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Ref.
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Embo J, 1993,
12,
2617-2624.
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PubMed id
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Abstract
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The Src-homology 3 (SH3) region is a protein domain consisting of approximately
60 residues. It occurs in a large number of eukaryotic proteins involved in
signal transduction, cell polarization and membrane--cytoskeleton interactions.
The function is unknown, but it is probably involved in specific
protein--protein interactions. Here we report the crystal structure of the SH3
domain of Fyn (a Src family tyrosine kinase) at 1.9 A resolution. The crystals
have two SH3 molecules per asymmetric unit. These two Fyn SH3 domains are not
related by a local twofold axis. The crystal structures of spectrin and Fyn SH3
domains as well as the solution structure of the Src SH3 domain show that these
all have the same basic fold. A protein domain which has the same topology as
SH3 is present in the prokaryotic regulatory enzyme BirA. The comparison between
the crystal structures of Fyn and spectrin SH3 domains shows that a conserved
surface patch, consisting mainly of aromatic residues, is flanked by two
hairpin-like loops (residues 94-104 and 114-118 in Fyn). These loops are
different in tyrosine kinase and spectrin SH3 domains. They could modulate the
binding properties of the aromatic surface.
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