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Title
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Crystal structure of a Src-homology 3 (SH3) domain.
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Authors
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A.Musacchio,
M.Noble,
R.Pauptit,
R.Wierenga,
M.Saraste.
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Ref.
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Nature, 1992,
359,
851-855.
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PubMed id
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Abstract
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The Src-homologous SH3 domain is a small domain present in a large number of
proteins that are involved in signal transduction, such as the Src protein
tyrosine kinase, or in membrane-cytoskeleton interactions, but the function of
SH3 is still unknown (reviewed in refs 1-3). Here we report the
three-dimensional structure at 1.8 A resolution of the SH3 domain of the
cytoskeletal protein spectrin expressed in Escherichia coli. The domain is a
compact beta-barrel made of five antiparallel beta-strands. The amino acids that
are conserved in the SH3 sequences are located close to each other on one side
of the molecule. This surface is rich in aromatic and carboxylic amino acids,
and is distal to the region of the molecule where the N and C termini reside and
where SH3 inserts into the alpha-spectrin chain. We suggest that a protein
ligand binds to this conserved surface of SH3.
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