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PDBsum entry 1kn3
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Protein binding
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PDB id
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1kn3
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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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The crystal structure of pebp-2, A homologue of the pebp/rkip family.
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Authors
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P.C.Simister,
M.J.Banfield,
R.L.Brady.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2002,
58,
1077-1080.
[DOI no: ]
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PubMed id
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Abstract
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Proteins from the PEBP (phosphatidylethanolamine-binding protein) family have
been identified in a wide variety of species and are thought to regulate a range
of intracellular signalling cascades. The rat homologue (known as RKIP; Raf-1
kinase inhibitor protein) has been shown to negatively regulate the MAP kinase
pathway through formation of inhibitory complexes with Raf-1 and MEK. The
crystal structure of a new, murine member of the PEBP family, termed mPEBP-2,
has been determined. On the basis of amino-acid homology, mPEBP-2 belongs to a
distinct subset of the mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to
be very similar in structure to other PEBP proteins from human, bovine and plant
sources. Regions of distinctive sequence associated with the PEBP-2 subset are
discussed with reference to this structure.
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Figure 2.
Figure 2 Stereoviews showing overlays of the mPEBP-2 and hPEBP-1
structures. (a) C^  trace
showing an overlay of the mPEBP-2 and hPEBP-1 structures. The
first 41 residues are coloured orange (mPEBP-2) and green
(hPEBP-1), highlighting the surface region where the greatest
sequence differences in the mammalian PEBP family are clustered.
The rest of the C^ trace
is coloured cyan (mPEBP-2) and purple (hPEBP-1). The
ligand-binding site is identified by the bound cacodylate ion
shown in CPK (from the hPEBP-1 structure). (b) Amino acids in
the ligand-binding site [mPEBP-2 bonds in cyan, hPEBP-1 bonds in
purple; bound cacodylate (from the hPEBP-1 structure) is also
shown].
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2002,
58,
1077-1080)
copyright 2002.
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