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PDBsum entry 1b4r
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Membrane protein
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PDB id
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1b4r
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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 structure of a pkd domain from polycystin-1: implications for polycystic kidney disease.
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Authors
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M.Bycroft,
A.Bateman,
J.Clarke,
S.J.Hamill,
R.Sandford,
R.L.Thomas,
C.Chothia.
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Ref.
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EMBO J, 1999,
18,
297-305.
[DOI no: ]
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PubMed id
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Abstract
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Most cases of autosomal dominant polycystic kidney disease (ADPKD) are the
result of mutations in the PKD1 gene. The PKD1 gene codes for a large
cell-surface glycoprotein, polycystin-1, of unknown function, which, based on
its predicted domain structure, may be involved in protein-protein and
protein-carbohydrate interactions. Approximately 30% of polycystin-1 consists of
16 copies of a novel protein module called the PKD domain. Here we show that
this domain has a beta-sandwich fold. Although this fold is common to a number
of cell-surface modules, the PKD domain represents a distinct protein family.
The tenth PKD domain of human and Fugu polycystin-1 show extensive conservation
of surface residues suggesting that this region could be a ligand-binding site.
This structure will allow the likely effects of missense mutations in a large
part of the PKD1 gene to be determined.
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Figure 7.
Figure 7 PKDd1 showing the conserved structurally important
sequence WDFGDGS. The figure was prepared using the program
Molscript (Kraulis, 1991).
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Figure 8.
Figure 8 (A) A structural alignment of the sequences of human
and Fugu PKD domain 10 (PKDd10) with that of human PKDd1. (B)
Schematic representation of the sequence conservation in the
sheets of PKDd10. The surface residues only are shown, in a view
looking at the molecule from the outside. The filled circles
represent residues pointing into the interior of the protein.
The C' -C -F -G sheet is shown in the same orientation as used
in Figure 3. The A -B -E sheet is shown with the entire molecule
rotated 180° about the y-axis. The human sequence is on the
left, the Fugu sequence on the right. Residues in the A -B -E
sheet that are putative glycosylation sites are shaded.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
297-305)
copyright 1999.
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