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PDBsum entry 1xf5
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Immune system
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PDB id
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1xf5
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Contents |
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16 a.a.
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220 a.a.
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218 a.a.
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71 a.a.
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67 a.a.
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References listed in PDB file
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Key reference
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Title
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Different crystal packing in FAB-Protein l semi-Disordered peptide complex.
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Authors
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R.Ménez,
N.G.Housden,
S.Harrison,
C.Jolivet-Reynaud,
M.G.Gore,
E.A.Stura.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2005,
61,
744-749.
[DOI no: ]
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PubMed id
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Abstract
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Proteins and peptides with variable degrees of disorder are a challenge for
protein crystallization. These may be completely disordered or just contain
regions with a high degree of mobility that may be represented by a multitude of
discretely defined conformations. These difficulties are not insurmountable, but
it may be unreasonable to expect a clean result from a structural point of view.
The complex between a murine monoclonal antibody (19D9D6) and a synthetic
peptide that encompasses the first 45 residues of the core protein of Hepatitis
C virus that is poorly structured in solution has been crystallized. In order to
make the crystallization possible, use was made of a single
immunoglobulin-binding domain of protein L from Peptostreptococcus magnus (PpL),
a bacterial protein that can bind the variable region (Fv) of a large population
of antibodies through its light chain with no interference with antibody-antigen
recognition. Crystals were obtained in different space groups where the size of
the cavity that accommodates the peptide is different, although many of the
crystal contacts and the overall lattice are preserved. The peptide can be
considered to be semi-disordered and the larger cavity accommodates a better
ordered peptide than the smaller one. The lattice is of interest for the design
of a scaffold system for the crystallization of peptide-tagged proteins since a
cavity that accommodates a disordered entity might be able to host ordered
proteins of the same size and shape as the cavity. Here, the differences between
the lattices formed by this trimolecular complex are described and it is
discussed how such a system may be adapted to the crystallization of
peptide-tagged proteins.
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Figure 2.
Figure 2
Omit map of peptide 2-45 in the complex with Fab' 19D9D6 (blue) and PpL (not shown). The
two peptides (red) do not adopt the same conformation and are not as well ordered within
and outside the recognition site. Peptide P (a) is fully occupied and ordered while
peptide Q (b) is not, possibly because of poor peptide availability.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
744-749)
copyright 2005.
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