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PDBsum entry 2kny
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Metal binding protein
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PDB id
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2kny
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References listed in PDB file
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Key reference
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Title
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Structure of the minimal interface between apoe and lrp.
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Authors
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M.Guttman,
J.H.Prieto,
T.M.Handel,
P.J.Domaille,
E.A.Komives.
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Ref.
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J Mol Biol, 2010,
398,
306-319.
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PubMed id
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Abstract
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Clusters of complement-type ligand-binding repeats (CRs) in the low-density
lipoprotein receptor (LDLR) family are thought to mediate the interactions with
their various ligands. Apolipoprotein E (ApoE), a key ligand for cholesterol
homeostasis, has been shown to interact with LDLR-related protein 1 (LRP)
through these clusters. The segment comprising the receptor-binding portion of
ApoE (residues 130-149) has been found to have a weak affinity for isolated CRs.
We have fused this region of ApoE to a high-affinity CR from LRP (CR17) for
structural elucidation of the complex. The interface reveals a motif that has
previously been observed in CR domains with other binding partners, but with
several novel features. Comparison to free CR17 reveals that very few structural
changes result from this binding event, but significant changes in intrinsic
dynamics are observed upon binding. NMR perturbation experiments suggest that
this interface may be similar to several other ligand interactions with LDLRs.
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