PDBsum entry 2kny

Metal binding protein

PDB id: 2kny

Contents

Protein chain

80 a.a. *

Metals

_CA

* Residue conservation analysis

PDB id:

2kny

Name:

Metal binding protein

Title:

Fusion construct of cr17 from lrp-1 and apoe residues 130-149

Structure:

Lrp-1, linker, apo-e. Chain: a. Fragment: fusion of lrp unp residues 2770-2817 and apo-e unp residues 147-167. Synonym: lrp, alpha-2-macroglobulin receptor, a2mr, apolipoprotein e receptor, apoer, low-density lipoprotein receptor-related protein 1 85 kda subunit, lrp-85, low-density lipoprotein receptor-related protein 1 515 kda subunit, lrp-515, low-density lipoprotein receptor- related protein 1 intracellular domain, lrpicd.

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.A.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:

08-Sep-09 Release date: 14-Apr-10

Protein chain

P02649  (APOE_HUMAN) -  Apolipoprotein E from Homo sapiens

Seq: 317 a.a.

Struc: 80 a.a.*

Protein chain

Q07954  (LRP1_HUMAN) -  Prolow-density lipoprotein receptor-related protein 1 from Homo sapiens

Seq: 4544 a.a.

Struc: 80 a.a.*

* PDB and UniProt seqs differ at 82 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.