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PDBsum entry 5hck
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References listed in PDB file
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Key reference
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Title
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Solution structure of the human hck sh3 domain and identification of its ligand binding site.
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Authors
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D.A.Horita,
D.M.Baldisseri,
W.Zhang,
A.S.Altieri,
T.E.Smithgall,
W.H.Gmeiner,
R.A.Byrd.
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Ref.
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J Mol Biol, 1998,
278,
253-265.
[DOI no: ]
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PubMed id
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Abstract
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SH3 domains are protein binding domains that occur widely among signal
transduction proteins. Here, we present the NMR-determined solution structure of
the SH3 domain from the cytoplasmic protein tyrosine kinase, Hck. Hck is
involved in a number of cell signal transduction pathways, frequently in
pathways associated with immune response. SH3 domains bind proteins via a
left-handed polyproline type II helix on the target protein. We have assessed
the structural impact of binding to a ligand through addition of a peptide
corresponding to a proline-rich region of a Hck target, the GTPase activating
protein of the Ras pathway. Ligand binding effects small structural changes and
stabilizes the SH3 domain structure. Also, we have compared the solution
structure of the Hck SH3 domain to the crystal structure of Hck, in which the
SH3 domain exhibits an intramolecular binding to an interdomain linker region.
These structures are interpreted as the apo- and holo- forms of the Hck SH3
domain.
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Figure 1.
Figure 1. Domain structure of human p60^hckand sequence and
secondary structural alignment for the Hck SH3 domain. Residues
listed in italics were excluded from the structure calculation.
Numbering for p59^hckstarts at p60^hckresidue 21.
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Figure 9.
Figure 9. Superimposition of residues W114 and I128 to V133
of the minimized average NMR structure (blue) with the
corresponding residues for the SH3 domain (red) and the PXXP
motif (green) from the Hck crystal structure (PDB entry 1ad5).
Superimposition of the SH3 domains was calculated to minimize
the RMSD for strands ba, bb, bc, and be.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1998,
278,
253-265)
copyright 1998.
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