PDBsum entry 1ypu

Immune system

PDB id: 1ypu

Contents

Protein chain

131 a.a. *

Waters ×290

* Residue conservation analysis

PDB id:

1ypu

Name:

Immune system

Title:

Human oxidized low density lipoprotein receptor lox-1 c2 space group

Structure:

Oxidised low density lipoprotein (lectin-like) receptor 1. Chain: a, b. Fragment: c-type lectin-like domain (residues 136-273). Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.05Å R-factor: 0.183 R-free: 0.238

Authors:

H.Park,F.G.Adsit,J.C.Boyington

Key ref:

H.Park et al. (2005). The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1. J Biol Chem, 280, 13593-13599. PubMed id: 15695803 DOI: 10.1074/jbc.M500768200

Date:

31-Jan-05 Release date: 08-Feb-05

Protein chains

P78380  (OLR1_HUMAN) -  Oxidized low-density lipoprotein receptor 1 from Homo sapiens

Seq: 273 a.a.

Struc: 131 a.a.

DOI no: 10.1074/jbc.M500768200

J Biol Chem 280:13593-13599 (2005)

PubMed id: 15695803

The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1.

H.Park, F.G.Adsit, J.C.Boyington.

ABSTRACT

The lectin-like oxidized low density lipoprotein receptor-1 (Lox-1) mediates the recognition and internalization of oxidatively modified low density lipoprotein by vascular endothelial cells. This interaction results in a number of pro-atherogenic cellular responses that probably play a significant role in the pathology of atherosclerosis. The 1.4 angstrom crystal structure of the extracellular C-type lectin-like domain of human Lox-1 reveals a heart-shaped homodimer with a ridge of six basic amino acids extending diagonally across the apolar top of Lox-1, a central hydrophobic tunnel that extends through the entire molecule, and an electrostatically neutral patch of 12 charged residues that resides next to the tunnel at each opening. Based on the arrangement of critical binding residues on the Lox-1 structure, we propose a binding mode for the recognition of modified low density lipoprotein and other Lox-1 ligands.

Selected figure(s)

Figure 2.
FIG. 2. The human Lox-1 tunnel. Stereoview of the tunnel outer molecular surface viewed from the top (a; orientation similar to Fig. 1b) and from the tunnel end (b; as in Fig. 1a). The semitransparent tunnel molecular surface is colorcoded with green for carbon, red for oxygen, and blue for nitrogen. Selected residues and bound dioxane are shown as stick models. c, stereoview of the interactions bound dioxane makes in the Lox-1 tunnel including the 1.4 Å 2F[o]-F[c] electron density map contoured to 1.0 . Hydrogen bonds are represented by dotted lines and the electron density for dioxane is colored dark blue for clarity.

Figure 4.
FIG. 4. Surface features of human Lox-1. a, molecular surface view of Lox-1 highlighting the acid-base patch on monomer A. A dotted line encloses the patch. Basic residues are blue, acid residues are red, nonpolar residues are brown, histidine is slate blue, and the rest are green. Top view (b) and side view (c) of the dimer (same orientations as in Fig. 1, b and a, respectively). The three conserved basic patches are outlined by dotted lines in c. Residues 210, 236, and 237 that have arginine or lysine side chains in ortholog Lox-1 structures are colored cyan in b and c.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 13593-13599) copyright 2005.

Figures were selected by an automated process.