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PDBsum entry 2knx

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protein metals links
Protein binding PDB id
2knx
Jmol
Contents
Protein chain
50 a.a. *
Metals
_CA
* Residue conservation analysis
PDB id:
2knx
Name: Protein binding
Title: Solution structure of complement repeat cr17 from lrp-1
Structure: Prolow-density lipoprotein receptor-related prote chain: a. Fragment: residues 2770-2817. Synonym: lrp, alpha-2-macroglobulin receptor, a2mr, apolipo receptor, apoer, low-density lipoprotein receptor-related p 85 kda subunit, lrp-85, low-density lipoprotein receptor-re protein 1 515 kda subunit, lrp-515, low-density lipoprotein related protein 1 intracellular domain, lrpicd. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: lrp1, a2mr, apr. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: M.Guttman,E.Komives
Key ref: M.Guttman et al. (2010). Structure of the minimal interface between ApoE and LRP. J Mol Biol, 398, 306-319. PubMed id: 20303980
Date:
07-Sep-09     Release date:   14-Apr-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q07954  (LRP1_HUMAN) -  Prolow-density lipoprotein receptor-related protein 1
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4544 a.a.
50 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
J Mol Biol 398:306-319 (2010)
PubMed id: 20303980  
 
 
Structure of the minimal interface between ApoE and LRP.
M.Guttman, J.H.Prieto, T.M.Handel, P.J.Domaille, E.A.Komives.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21080234 S.Y.Morita, A.Sakurai, M.Nakano, S.Kitagawa, and T.Handa (2011).
Presence of apolipoprotein C-III attenuates apolipoprotein E-mediated cellular uptake of cholesterol-containing lipid particles by HepG2 cells.
  Lipids, 46, 323-332.  
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