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PDBsum entry 1bv8
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Protein binding
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PDB id
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1bv8
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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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Nmr solution structure of complement-Like repeat cr8 from the low density lipoprotein receptor-Related protein.
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Authors
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W.Huang,
K.Dolmer,
P.G.Gettins.
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Ref.
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J Biol Chem, 1999,
274,
14130-14136.
[DOI no: ]
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PubMed id
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Abstract
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The low density lipoprotein receptor-related protein is a member of the low
density lipoprotein receptor family and contains clusters of cysteine-rich
complement-like repeats of about 42 residues that are present in all members of
this family of receptors. These clusters are thought to be the principal binding
sites for protein ligands. We have expressed one complement-like repeat, CR8,
from the cluster in lipoprotein receptor-related protein that binds certain
proteinase inhibitor-proteinase complexes and used three-dimensional NMR on the
13C/15N-labeled protein to determine the structure in solution of the
calcium-bound form. The structure is very similar in overall fold to repeat 5
from the low density lipoprotein receptor (LB5), with backbone root mean square
deviation of 1.5 A. The calcium-binding site also appears to be homologous, with
four carboxyl and two backbone carbonyl ligands. However, differences in primary
structure are such that equivalent surfaces that might represent the binding
interfaces are very different from one another, indicating that different
domains will have very different ligand specificities.
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Figure 6.
Fig. 6. Comparison of the calcium coordination sites of
CR8 and LB5. The views are the same as that in Fig. 5. The
coordinates for the LB5 representation were obtained from
Brookhaven Protein Data Bank, from deposition 1ajj. Because the
coordinates of Ca^2+ are not provided in 1ajj, the position was
inferred from the published ligand-calcium separations.
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Figure 7.
Fig. 7. Structural comparison of the backbones of CR8
(dark line) and LB5 (light line) using deposited coordinates of
LB5 and the lowest energy NMR structure of CR8 from those
depicted in Fig. 4. Statistics for the comparison are presented
in Table II. A, best overlay of the whole structures. B, best
overlay of the N-terminal  -sheet-containing
region. C, best overlay of the calcium-binding region.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(1999,
274,
14130-14136)
copyright 1999.
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