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PDBsum entry 1a6p
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Cell adhesion
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PDB id
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1a6p
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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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Engineering an intertwined form of cd2 for stability and assembly.
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Authors
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A.J.Murray,
J.G.Head,
J.J.Barker,
R.L.Brady.
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Ref.
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Nat Struct Biol, 1998,
5,
778-782.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
0%.
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Abstract
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The amino-terminal domain of CD2 has the remarkable ability to fold in two ways:
either as a monomer or as an intertwined, metastable dimer. Here we show that it
is possible to differentially stabilize either fold by engineering the CD2
sequence, mimicking random mutagenesis events that could occur during molecular
evolution. Crystal structures of a hinge-deletion mutant, which is stable as an
intertwined dimer, reveal domain rotations that enable the protein to further
assemble to a tetramer. These results demonstrate that a variety of folds can be
adopted by a single polypeptide sequence, and provide guidance for the design of
proteins capable of further assembly.
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Figure 3.
Figure 3. Stereo C  traces
depicting the crystal structures of a, the wild type intertwined
dimer, with the enclosed hydrophilic interface, and b, in a
similar orientation, the  46
47
deletion mutant intertwined dimer in the P4[3] crystal form
(forms I and II). The hydrophilic interface is now in an
'exposed' conformation. When crystallized under high-salt
conditions (crystal form III) c, this same structure is also
observed, but now a tetramer is formed in which a second
intertwined dimer binds with both hydrophilic interfaces
interlocked to form a central, extended  -barrel.
The spheres identify the location of equivalent residues
(position 49) central to each polypeptide chain, illustrating
their close proximity in the tetramer and hence the feasibility
of further exchange of polypeptide chains in this region to form
a fully intertwined tetramer.
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Figure 4.
Figure 4. Stereo view of electron density (3F[o] - 2F[c]
coefficients, contoured at 1  )
from the hinge region residues in the P4[3], type I, crystal
form of the 46
47
deletion mutant intertwined dimer. The deletion site is
adjacent to the proline in the center of the figure.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
778-782)
copyright 1998.
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